Yeast PPR proteins, watchdogs of mitochondrial gene expression

Herbert, Christopher J; Golik, Pawel; Bonnefoy, Nathalie

doi:10.4161/rna.25392

Cited by 54RNA Research and SplicingMitochondrial Function and PathologyRNA and protein synthesis mechanisms

Yeast PPR proteins, watchdogs of mitochondrial gene expression

Open access

Herbert, Christopher J, Golik, Pawel, Bonnefoy, Nathalie·2013·RNA Biology

DOI 10.4161/rna.25392PMC PMC3858431

Open this paper in CoChat — free account Open PDF

Abstract

PPR proteins are a family of ubiquitous RNA-binding factors, found in all the Eukaryotic lineages, and are particularly numerous in higher plants. According to recent bioinformatic analyses, yeast genomes encode from 10 (in S. pombe) to 15 (in S. cerevisiae) PPR proteins. All of these proteins are mitochondrial and very often interact with the mitochondrial membrane. Apart from the general factors, RNA polymerase and RNase P, most yeast PPR proteins are involved in the stability and/or translation of mitochondrially encoded RNAs. At present, some information concerning the target RNA(s) of most of these proteins is available, the next challenge will be to refine our understanding of the function of the proteins and to resolve the yeast PPR-RNA-binding code, which might differ significantly from the plant PPR code.

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

Integrity signals

Registry

Crossref · 10.4161/rna.25392

Cites

106 of 106 references verified0 citation errors · 0 not checkable

Statistics

Claims the paper makes

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

Thirteen putative C. albicans PPR proteins were identified using the SCIPHER algorithm by Lipinski et al. (2011), and 9 of them show clear orthology to well-characterized PPR proteins of S. cerevisiae and S. pombe.
“Thirteen putative C. albicans PPR proteins were identified using the SCIPHER algorithm by Lipinski et al. (2011), and 9 of them show clear orthology to well-characterized PPR proteins of S. cerevisiae and S. pombe (CaAep3p, CaAep2p, CaDmr1p, CaRpo41p, CaPet111p, CaPet309p, CaAtp22p, CaRmd9p, and CaCbp1p) (Kühl et al. 2011; Lipinski et al. 2011; Herbert et al. 2013).”
From Candida albicans PPR proteins are required for the expression of respiratory Complex I subunits (2024) · cites this paper as Herbert et al. 2013
The SCIPHER algorithm tailored for the identification of new members of this family in yeasts does not recognize numerous μ-helical repeats as statistically significant PPR motifs.
“The SCIPHER algorithm tailored for the identification of new members of this family in yeasts does not recognize numerous µ-helical repeats as statistically significant PPR motifs (Herbert et al. 2013).”
From Candida albicans PPR proteins are required for the expression of respiratory Complex I subunits (2024) · cites this paper as Herbert et al. 2013

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

The Pfam Protein Families Database
Bateman, A. G. (2002) · Nucleic Acids Research · doi:10.1093/nar/30.1.276 · Cited by 14,062 · see citing works
Profile hidden Markov models
Eddy, S. R. (1998) · Bioinformatics · doi:10.1093/bioinformatics/14.9.755 · Cited by 5,515 · see citing works
Global analysis of protein localization in budding yeast
Huh, W.-K., Falvo, J. V., Gerke, L. C., Carroll, A. S., Howson, R. W., Weissman, J. S., & O'Shea, E. K. (2003) · Nature · doi:10.1038/nature02026 · Cited by 4,248 · see citing works
The Pfam protein families database
Finn, R. D., Mistry, J., Tate, J., Coggill, P., Heger, A., Pollington, J. E., Gavin, O. L., Gunasekaran, P., Ceric, G., Forslund, K., et al. (2010) · Nucleic Acids Research · doi:10.1093/nar/gkp985 · Cited by 2,694 · see citing works
The RNA moiety of ribonuclease P is the catalytic subunit of the enzyme
Guerrier-Takada, C., Gardiner, K., Marsh, T., Pace, N., & Altman, S. (1983) · Cell · doi:10.1016/0092-8674(83)90117-4 · Cited by 2,684 · see citing works
Computational method to predict mitochondrially imported proteins and their targeting sequences.
Claros, M. G., & Vincens, P. (1996) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1996.00779.x · Cited by 1,736 · see citing works
The proteome of Saccharomyces cerevisiae mitochondria
Sickmann, A., Reinders, J., Wagner, Y., Joppich, C., Zahedi, R. P., Meyer, H. E., Schönfisch, B., Perschil, I., Chacińska, A., Guiard, B., et al. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2135385100 · Cited by 895 · see citing works
The PPR motif – a TPR-related motif prevalent in plant organellar proteins
Small, I., & Peeters, N. M. (2000) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(99)01520-0 · Cited by 839 · see citing works
Identification of a gene causing human cytochrome c oxidase deficiency by integrative genomics
Mootha, V. K., Lepage, P., Miller, K., Bunkenborg, J., Reich, M. M., Hjerrild, M., DelMonte, T. A., Villeneuve, A., SLADEK, R. M., Xu, F., et al. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.242716699 · Cited by 578 · see citing works
A Combinatorial Amino Acid Code for RNA Recognition by Pentatricopeptide Repeat Proteins
Barkan, A., Rojas, M., Fujii, S., Yap, A., Chong, Y. S., Bond, C. S., & Small, I. (2012) · PLoS Genetics · doi:10.1371/journal.pgen.1002910 · Cited by 538 · see citing works
Comparative functional genomics of the fission yeasts
Rhind, N., Chen, Z., Yassour, M., Thompson, D. A., Haas, B. J., Habib, N., Wapinski, I., Roy, S., Lin, M. F., Heiman, D. I., et al. (2011) · Science · doi:10.1126/science.1203357 · Cited by 484 · see citing works
The complete sequence of the mitochondrial genome of Saccharomyces cerevisiae
Foury, F., Roganti, T., Lecrenier, N., & Purnelle, B. (1998) · FEBS Letters · doi:10.1016/s0014-5793(98)01467-7 · Cited by 434 · see citing works
Toward the Complete Yeast Mitochondrial Proteome: Multidimensional Separation Techniques for Mitochondrial Proteomics
Reinders, J., Zahedi, R. P., Pfanner, N., Meisinger, C., & Sickmann, A. (2006) · Journal of Proteome Research · doi:10.1021/pr050477f · Cited by 394 · see citing works
Incompatibility of Nuclear and Mitochondrial Genomes Causes Hybrid Sterility between Two Yeast Species
Lee, H., Chou, J., Cheong, L., Chang, N.-H., Yang, S.-Y., & Leu, J. (2008) · Cell · doi:10.1016/j.cell.2008.10.047 · Cited by 384 · see citing works
LRPPRC is necessary for polyadenylation and coordination of translation of mitochondrial mRNAs
Ruzzenente, B., Metodiev, M. D., Wredenberg, A., Bratić, A. M., Park, C. B., Cámara, Y., Milenkovic, D., Zickermann, V., Wibom, R., Hultenby, K. R., et al. (2011) · The EMBO Journal · doi:10.1038/emboj.2011.392 · Cited by 350 · see citing works
Mechanism of RNA stabilization and translational activation by a pentatricopeptide repeat protein
Prikryl, J., Rojas, M., Schuster, G., & Barkan, A. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1012076108 · Cited by 298 · see citing works
When protein folding is simplified to protein coiling: the continuum of solenoid protein structures
Kobe, B., & Kajava, A. V. (2000) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(00)01667-4 · Cited by 281 · see citing works
Structure of human mitochondrial RNA polymerase
Ringel, R., Sologub, M., Morozov, Y. I., Litonin, D., Cramer, P., & Temiakov, D. (2011) · Nature · doi:10.1038/nature10435 · Cited by 235 · see citing works
HMM Logos for visualization of protein families
Schuster‐Böckler, B., Schultz, J., & Rahmann, S. (2004) · BMC Bioinformatics · doi:10.1186/1471-2105-5-7 · Cited by 228 · see citing works
TPRpred: a tool for prediction of TPR-, PPR- and SEL1-like repeats from protein sequences
Ranganathappa, M. K., Lupas, A. N., & Söding, J. (2007) · BMC Bioinformatics · doi:10.1186/1471-2105-8-2 · Cited by 226 · see citing works
The product of the nuclear gene PET309 is required for translation of mature mRNA and stability or production of intron‐containing RNAs derived from the mitochondrial COX1 locus of Saccharomyces cerevisiae.
Manthey, G. M., & McEwen, J. E. (1995) · The EMBO Journal · doi:10.1002/j.1460-2075.1995.tb00074.x · Cited by 224 · see citing works
LRPPRC/SLIRP suppresses PNPase-mediated mRNA decay and promotes polyadenylation in human mitochondria
Chujo, T., Ohira, T., Sakaguchi, Y., Goshima, N., Nomura, N., Nagao, A., & Suzuki, T. (2012) · Nucleic Acids Research · doi:10.1093/nar/gks506 · Cited by 203 · see citing works
Expression of a recoded nuclear gene inserted into yeast mitochondrial DNA is limited by mRNA-specific translational activation.
Steele, D. F., Butler, C. A., & Fox, T. D. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.11.5253 · Cited by 181 · see citing works
The role of the LRPPRC (leucine-rich pentatricopeptide repeat cassette) gene in cytochrome oxidase assembly: mutation causes lowered levels of COX (cytochrome c oxidase) I and COX III mRNA
Xu, F., Morin, C., Mitchell, G. A., Ackerley, C. A., & Robinson, B. H. (2004) · Biochemical Journal · doi:10.1042/bj20040469 · Cited by 172 · see citing works
An mRNA maturase is encoded by the first intron of the mitochondrial gene for the subunit I of cytochrome oxidase in S. cerevisiae
Carignani, G., Groudinsky, O., Frezza, D., Schiavon, E., Bergantino, E., & Słonimski, P. P. (1983) · Cell · doi:10.1016/0092-8674(83)90106-x · Cited by 168 · see citing works
Interactions amongCOX1,COX2, andCOX3mRNA-specific Translational Activator Proteins on the Inner Surface of the Mitochondrial Inner Membrane ofSaccharomyces cerevisiae
Naithani, S., Saracco, S. A., Butler, C. A., & Fox, T. D. (2003) · Molecular Biology of the Cell · doi:10.1091/mbc.e02-08-0490 · Cited by 159 · see citing works
PET111, a Saccharomyces cerevisiae Nuclear Gene Required for Translation of the Mitochondrial mRNA Encoding Cytochrome c Oxidase Subunit II
Poutre, C. G., & Fox, T. D. (1987) · Genetics · doi:10.1093/genetics/115.4.637 · Cited by 142 · see citing works
Multiple Molecular Mechanisms Cause Reproductive Isolation between Three Yeast Species
Chou, J., Hung, Y.-S., Lin, K.-H., Lee, H.-Y., & Leu, J. (2010) · PLoS Biology · doi:10.1371/journal.pbio.1000432 · Cited by 141 · see citing works
Cox18p Is Required for Export of the Mitochondrially EncodedSaccharomyces cerevisiaeCox2p C-Tail and Interacts with Pnt1p and Mss2p in the Inner Membrane
Saracco, S. A., & Fox, T. D. (2002) · Molecular Biology of the Cell · doi:10.1091/mbc.01-12-0580 · Cited by 132 · see citing works
Evidence for a Pro-oxidant Intermediate in the Assembly of Cytochrome Oxidase
Khalimonchuk, O., Bird, A. J., & Winge, D. R. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m702379200 · Cited by 124 · see citing works
A recurring theme in protein engineering: the design, stability and folding of repeat proteins
Main, E. R. G., Lowe, A. R., Mochrie, S. G. J., Jackson, S. P., & Regan, L. (2005) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2005.07.003 · Cited by 122 · see citing works
Mitochondrial ribonuclease P structure provides insight into the evolution of catalytic strategies for precursor-tRNA 5′ processing
Howard, M. J., Lim, W. H., Fierke, C. A., & Koutmos, M. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1209062109 · Cited by 119 · see citing works
Genetic Control of Recombination Partner Preference in Yeast Meiosis: Isolation and Characterization of Mutants Elevated for Meiotic Unequal Sister-Chromatid Recombination
Thompson, D. A., & Stahl, F. W. (1999) · Genetics · doi:10.1093/genetics/153.2.621 · Cited by 119 · see citing works
Speciation through cytonuclear incompatibility: Insights from yeast and implications for higher eukaryotes
Chou, J., & Leu, J. (2010) · BioEssays · doi:10.1002/bies.200900162 · Cited by 109 · see citing works
Pet111p, an Inner Membrane-bound Translational Activator That Limits Expression of the Saccharomyces cerevisiaeMitochondrial Gene COX2
Green-Willms, N. S., Butler, C. A., Dunstan, H. M., & Fox, T. D. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m009856200 · Cited by 106 · see citing works
Pentatricopeptide repeat domain protein 3 associates with the mitochondrial small ribosomal subunit and regulates translation
Davies, S. M. K., Rackham, O., Shearwood, A.-M. J., Hamilton, K. L., Narsai, R., Whelan, J., & Filipovska, A. (2009) · FEBS Letters · doi:10.1016/j.febslet.2009.04.048 · Cited by 105 · see citing works
Human Mitochondrial Ribosomal Protein MRPL12 Interacts Directly with Mitochondrial RNA Polymerase to Modulate Mitochondrial Gene Expression
Wang, Z., Cotney, J. L., & Shadel, G. S. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m700461200 · Cited by 100 · see citing works
The Pentatricopeptide Repeats Present in Pet309 Are Necessary for Translation but Not for Stability of the Mitochondrial COX1 mRNA in Yeast
Tavares-Carreón, F., Camacho‐Villasana, Y., Zamudio‐Ochoa, A., Shingú-Vázquez, M., Torres‐Larios, A., & Pérez-Martı́nez, X. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m708437200 · Cited by 98 · see citing works
Pentatricopeptide Repeat Proteins in Trypanosoma brucei Function in Mitochondrial Ribosomes
Pusnik, M., Small, I., Read, L. K., Fabbro, T., & Schneider, A. (2007) · Molecular and Cellular Biology · doi:10.1128/mcb.00708-07 · Cited by 98 · see citing works
Nam1p, a Protein Involved in RNA Processing and Translation, Is Coupled to Transcription through an Interaction with Yeast Mitochondrial RNA Polymerase
Rodeheffer, M. S., Boone, B. E., Bryan, A., & Shadel, G. S. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m009901200 · Cited by 95 · see citing works
The Cbp3–Cbp6 complex coordinates cytochrome b synthesis with bc1 complex assembly in yeast mitochondria
Gruschke, S., Römpler, K., Hildenbeutel, M., Kehrein, K., Kühl, I., Bonnefoy, N., & Ott, M. (2012) · The Journal of Cell Biology · doi:10.1083/jcb.201206040 · Cited by 92 · see citing works
Self-citation
Dual Functions of Mss51 Couple Synthesis of Cox1 to Assembly of CytochromecOxidase inSaccharomyces cerevisiaeMitochondria
Pérez-Martı́nez, X., Butler, C. A., Shingú-Vázquez, M., & Fox, T. D. (2009) · Molecular Biology of the Cell · doi:10.1091/mbc.e09-06-0522 · Cited by 92 · see citing works
Mechanistic Insight into Pentatricopeptide Repeat Proteins as Sequence-Specific RNA-Binding Proteins for Organellar RNAs in Plants
Nakamura, T., Yagi, Y., & Kobayashi, K. (2012) · Plant and Cell Physiology · doi:10.1093/pcp/pcs069 · Cited by 88 · see citing works
F 1 -dependent translation of mitochondrially encoded Atp6p and Atp8p subunits of yeast ATP synthase
Rak, M., & Tzagoloff, A. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0910351106 · Cited by 86 · see citing works
Pentatricopeptide repeat domain protein 1 lowers the levels of mitochondrial leucine tRNAs in cells
Rackham, O., Davies, S. M. K., Shearwood, A.-M. J., Hamilton, K. L., Whelan, J., & Filipovska, A. (2009) · Nucleic Acids Research · doi:10.1093/nar/gkp627 · Cited by 86 · see citing works
In vivo analysis of mutated initiation codons in the mitochondrial COX2 gene of Saccharomyces cerevisiae fused to the reporter gene ARG8 m reveals lack of downstream reinitiation
Bonnefoy, N., & Fox, T. D. (2000) · Molecular and General Genetics MGG · doi:10.1007/pl00008646 · Cited by 83 · see citing works
Self-citation
PET111 acts in the 5'-leader of the Saccharomyces cerevisiae mitochondrial COX2 mRNA to promote its translation.
Mulero, J. J., & Fox, T. D. (1993) · Genetics · doi:10.1093/genetics/133.3.509 · Cited by 78 · see citing works
Mitochondrial Translation of Saccharomyces cerevisiae COX2 mRNA Is Controlled by the Nucleotide Sequence Specifying the Pre-Cox2p Leader Peptide
Bonnefoy, N., Bsat, N., & Fox, T. D. (2001) · Molecular and Cellular Biology · doi:10.1128/mcb.21.7.2359-2372.2001 · Cited by 77 · see citing works
Self-citation
A Heme-Sensing Mechanism in the Translational Regulation of Mitochondrial Cytochrome c Oxidase Biogenesis
Soto, I. C., Fontanesi, F., Myers, R. S., Hamel, P. P., & Barrientos, A. (2012) · Cell Metabolism · doi:10.1016/j.cmet.2012.10.018 · Cited by 76 · see citing works
Regulation of poly(A) site choice of several yeast mRNAs
Sparks, K. A., & Dieckmann, C. L. (1998) · Nucleic Acids Research · doi:10.1093/nar/26.20.4676 · Cited by 75 · see citing works
Genetic conservation versus variability in mitochondria: the architecture of the mitochondrial genome in the petite-negative yeast Schizosaccharomyces pombe
Schäfer, B. (2003) · Current Genetics · doi:10.1007/s00294-003-0404-5 · Cited by 74 · see citing works
Alteration of the Saccharomyces cerevisiae COX2 mRNA 5'-untranslated leader by mitochondrial gene replacement and functional interaction with the translational activator protein PET111.
Mulero, J. J., & Fox, T. D. (1993) · Molecular Biology of the Cell · doi:10.1091/mbc.4.12.1327 · Cited by 74 · see citing works
The Saccharomyces cerevisiae Pet309 protein is embedded in the mitochondrial inner membrane
Manthey, G. M., Przybyla‐Zawislak, B., & McEwen, J. E. (1998) · European Journal of Biochemistry · doi:10.1046/j.1432-1327.1998.2550156.x · Cited by 71 · see citing works
Nuclear mutations in the petite-negative yeast Schizosaccharomyces pombe allow growth of cells lacking mitochondrial DNA.
Haffter, P., & Fox, T. D. (1992) · Genetics · doi:10.1093/genetics/131.2.255 · Cited by 71 · see citing works
The Neurospora crassa cya-5 nuclear gene encodes a protein with a region of homology to the Saccharomyces cerevisiae PET309 protein and is required in a post-transcriptional step for the expression of the mitochondrially encoded COXI protein
Coffin, J. W., Dhillon, R., Ritzel, R. G., & Nargang, F. E. (1997) · Current Genetics · doi:10.1007/s002940050277 · Cited by 68 · see citing works
Revisiting the yeast PPR proteins–application of an iterative hidden Markov model algorithm reveals new members of the rapidly evolving family
Lipinski, K. A., Puchta, O., Surendranath, V., Kudla, M., & Golik, P. (2011) · Molecular Biology and Evolution · doi:10.1093/molbev/msr120 · Cited by 62 · see citing works
Self-citation
Aep3p Stabilizes the Mitochondrial Bicistronic mRNA Encoding Subunits 6 and 8 of the H+-translocating ATP Synthase of Saccharomyces cerevisiae
Ellis, T. P., Helfenbein, K. G., Tzagoloff, A., & Dieckmann, C. L. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m314162200 · Cited by 61 · see citing works
The mitochondrial message-specific mRNA protectors Cbp1 and Pet309 are associated in a high-molecular weight complex
Krause, K., Lopes de Souza, R., Roberts, D. G. W., & Dieckmann, C. L. (2004) · Molecular Biology of the Cell · doi:10.1091/mbc.e04-02-0126 · Cited by 60 · cited 1× · see citing works
“This would be consistent with the observation that Cbp1 interacts with the COX1 translational activator Pet309 (Table 2).(50) Like AEP2, CBP1 is transcribed as a full-length transcript able to encode the normal Cbp1 protein, and a truncated transcript that cannot produce Cbp1.”
Background
Molecular basis of the ‘box effect’
Labouesse, M., Netter, P., & Schroeder, R. (1984) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1984.tb08434.x · Cited by 59 · see citing works
In Vivo Analysis of Saccharomyces cerevisiae COX2 mRNA 5′-Untranslated Leader Functions in Mitochondrial Translation Initiation and Translational Activation
Dunstan, H. M., Green-Willms, N. S., & Fox, T. D. (1997) · Genetics · doi:10.1093/genetics/147.1.87 · Cited by 58 · see citing works
A genome wide study in fission yeast reveals nine PPR proteins that regulate mitochondrial gene expression
Kühl, I., Dujeancourt, L., Gaisne, M., Herbert, C. J., & Bonnefoy, N. (2011) · Nucleic Acids Research · doi:10.1093/nar/gkr511 · Cited by 58 · see citing works
Self-citation
The role of mammalian PPR domain proteins in the regulation of mitochondrial gene expression
Rackham, O., & Filipovska, A. (2011) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2011.10.007 · Cited by 58 · see citing works
RNA maturation in mitochondria of S. cerevisiae and S. pombe
Schäfer, B. (2005) · Gene · doi:10.1016/j.gene.2005.03.032 · Cited by 56 · see citing works
Properties of two nuclear pet mutants affecting expression of the mitochondrial oli1 gene of Saccharomyces cerevisiae
Payne, M. J., Schweizer, E., & Lukins, H. B. (1991) · Current Genetics · doi:10.1007/bf00309594 · Cited by 53 · see citing works
Divergence of the mitochondrial leucyl tRNA synthetase genes in two closely related yeasts Saccharomyces cerevisiae and Saccharomyces douglasii: A paradigm of incipient evolution
Herbert, C. J., Dujardin, G., Labouesse, M., & Słonimski, P. P. (1988) · Molecular and General Genetics MGG · doi:10.1007/bf00339595 · Cited by 51 · see citing works
Self-citation
Rmd9p Controls the Processing/Stability of Mitochondrial mRNAs and Its Overexpression Compensates for a Partial Deficiency of Oxa1p in Saccharomyces cerevisiae
Nouet, C., Bourens, M., Hlaváček, O., Marsy, S., Lemaire, C., & Dujardin, G. (2006) · Genetics · doi:10.1534/genetics.106.063883 · Cited by 51 · see citing works
The Saccharomyces cerevisiae ATP22 Gene Codes for the Mitochondrial ATPase Subunit 6-Specific Translation Factor
Zeng, X., Hourset, A., & Tzagoloff, A. (2006) · Genetics · doi:10.1534/genetics.106.065821 · Cited by 49 · see citing works
Genetic Transformation of Saccharomyces cerevisiae and Chlamydomonas reinhardtii Mitochondria
Bonnefoy, N., Remacle, C., & Fox, T. D. (2007) · Methods in cell biology · doi:10.1016/s0091-679x(06)80026-9 · Cited by 48 · see citing works
Self-citation
ATP13, a nuclear gene of Saccharomyces cerevisiae essential for the expression of subunit 9 of the mitochondrial ATPase
Ackerman, S. H., Gatti, D. L., Gellefors, P., Douglas, M. G., & Tzagoloff, A. (1991) · FEBS Letters · doi:10.1016/0014-5793(91)80124-l · Cited by 47 · see citing works
Cbp1 Is Required for Translation of the Mitochondrial Cytochromeb mRNA of Saccharomyces cerevisiae
Islas-Osuna, M. A., Ellis, T. P., Marnell, L. L., Mittelmeier, T. M., & Dieckmann, C. L. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m206132200 · Cited by 47 · see citing works
ATP22, a Nuclear Gene Required for Expression of the F0 Sector of Mitochondrial ATPase in Saccharomyces cerevisiae
Helfenbein, K. G., Ellis, T. P., Dieckmann, C. L., & Tzagoloff, A. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m301679200 · Cited by 46 · see citing works
Saccharomyces cerevisiae Positive Regulatory Gene PET111 Encodes a Mitochondrial Protein That Is Translated from an mRNA with a Long 5′ Leader
Strick, C. A., & Fox, T. D. (1987) · Molecular and Cellular Biology · doi:10.1128/mcb.7.8.2728-2734.1987 · Cited by 45 · see citing works
Sls1p Is a Membrane-Bound Regulator of Transcription-Coupled Processes Involved in Saccharomyces cerevisiae Mitochondrial Gene Expression
Bryan, A. C., Rodeheffer, M. S., Wearn, C. M., & Shadel, G. S. (2002) · Genetics · doi:10.1093/genetics/160.1.75 · Cited by 45 · see citing works
Mechanism of transcription initiation by the yeast mitochondrial RNA polymerase
Deshpande, A. P., & Patel, S. S. (2012) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2012.02.003 · Cited by 44 · see citing works
Reduced but accurate translation from a mutant AUA initiation codon in the mitochondrial COX2 mRNA of Saccharomyces cerevisiae
Mulero, J. J., & Fox, T. D. (1994) · Molecular and General Genetics MGG · doi:10.1007/bf00281787 · Cited by 42 · see citing works
Balance between Transcription and RNA Degradation Is Vital forSaccharomyces cerevisiaeMitochondria: Reduced Transcription Rescues the Phenotype of Deficient RNA Degradation
Rogowska, A., Puchta, O., Czarnecka, A. M., Kaniak, A., Stępień, P. P., & Golik, P. (2005) · Molecular Biology of the Cell · doi:10.1091/mbc.e05-08-0796 · Cited by 41 · see citing works
Self-citation
The yeast CBP1 gene produces two differentially regulated transcripts by alternative 3'-end formation.
Mayer, S. A., & Dieckmann, C. L. (1989) · Molecular and Cellular Biology · doi:10.1128/mcb.9.10.4161 · Cited by 40 · see citing works
Suppression of a Nuclear aep2 Mutation in Saccharomyces cerevisiae by a Base Substitution in the 5′-Untranslated Region of the Mitochondrial oli1 Gene Encoding Subunit 9 of ATP Synthase
Ellis, T. P., Lukins, H. B., Nagley, P., & Corner, B. E. (1999) · Genetics · doi:10.1093/genetics/151.4.1353 · Cited by 40 · see citing works
Translation Initiation inSaccharomyces cerevisiaeMitochondria: Functional Interactions Among Mitochondrial Ribosomal Protein Rsm28p, Initiation Factor 2, Methionyl-tRNA-Formyltransferase and Novel Protein Rmd9p
Williams, E. H., Butler, C. A., Bonnefoy, N., & Fox, T. D. (2006) · Genetics · doi:10.1534/genetics.106.064576 · Cited by 40 · see citing works
Self-citation
Characterization of a second nuclear gene, AEP1, required for expression of the mitochondrial OLI1 gene in Saccharomyces cerevisiae
Payne, M. J., Finnegan, P. M., Smooker, P. M., & Lukins, H. B. (1993) · Current Genetics · doi:10.1007/bf00324676 · Cited by 39 · see citing works
Relocation of the unusual VAR1 gene from the mitochondrion to the nucleus
Sanchirico, M. E., Tzellas, A., Mason, T. L., Fox, T. D., Conrad-Webb, H., & Perlman, P. S. (1995) · Biochemistry and Cell Biology · doi:10.1139/o95-106 · Cited by 37 · see citing works
Yeast mitochondrial RNase P, RNase Z and the RNA degradosome are part of a stable supercomplex
Daoud, R., Forget, L., & Lang, B. F. (2011) · Nucleic Acids Research · doi:10.1093/nar/gkr941 · Cited by 37 · see citing works
DMR1 (CCM1/YGR150C) of Saccharomyces cerevisiae Encodes an RNA-Binding Protein from the Pentatricopeptide Repeat Family Required for the Maintenance of the Mitochondrial 15S Ribosomal RNA
Puchta, O., Lubas, M., Lipinski, K. A., Piatkowski, J., Malecki, M., & Golik, P. (2010) · Genetics · doi:10.1534/genetics.110.113969 · Cited by 33 · see citing works
Self-citation
Highly Diverged Homologs of Saccharomyces cerevisiae Mitochondrial mRNA-Specific Translational Activators Have Orthologous Functions in Other Budding Yeasts
Costanzo, M. C., Bonnefoy, N., Williams, E. H., Clark-Walker, G. D., & Fox, T. D. (2000) · Genetics · doi:10.1093/genetics/154.3.999 · Cited by 32 · see citing works
Self-citation
Nuclear Control of the Messenger RNA Expression for Mitochondrial ATPase Subunit 9 in a New Yeast Mutant
Ziaja, K., Michaelis, G., & Lisowsky, T. (1993) · Journal of Molecular Biology · doi:10.1006/jmbi.1993.1095 · Cited by 32 · see citing works
Identification of proteins associated with the yeast mitochondrial RNA polymerase by tandem affinity purification
Markov, D. A., Savkina, M. V., Anikin, M., Campo, M. D., Ecker, K., Lambowitz, A. M., Gnore, J. P. D., & McAllister, W. T. (2009) · Yeast · doi:10.1002/yea.1672 · Cited by 30 · see citing works
The 3′ Ends of Mature Transcripts Are Generated by a Processosome Complex in Fission Yeast Mitochondria
Hoffmann, B., Nickel, J., Speer, F., & Schafer, B. (2008) · Journal of Molecular Biology · doi:10.1016/j.jmb.2008.01.038 · Cited by 30 · see citing works
Rpm2p, a protein subunit of mitochondrial RNase P, physically and genetically interacts with cytoplasmic processing bodies
Stribinskis, V., & Ramos, K. S. (2007) · Nucleic Acids Research · doi:10.1093/nar/gkm023 · Cited by 29 · see citing works
Ccm1p/Ygr150cp, a pentatricopeptide repeat protein, is essential to remove the fourth intron of both COB and COX1 pre-mRNAs in Saccharomyces cerevisiae
Moreno, J. I., Buie, K. S., Price, R. E., & Piva, M. A. (2009) · Current Genetics · doi:10.1007/s00294-009-0260-z · Cited by 28 · see citing works
Genetic Evidence for Interaction between Cbp1 and Specific Nucleotides in the 5′ Untranslated Region of Mitochondrial Cytochrome b mRNA in Saccharomyces cerevisiae
Chen, W., & Dieckmann, C. L. (1997) · Molecular and Cellular Biology · doi:10.1128/mcb.17.11.6203 · Cited by 28 · see citing works
Overexpression of the COX2 translational activator, Pet111p, prevents translation of COX1 mRNA and cytochrome c oxidase assembly in mitochondria of Saccharomyces cerevisiae
Fiori, A., Pérez-Martı́nez, X., & Fox, T. D. (2005) · Molecular Microbiology · doi:10.1111/j.1365-2958.2005.04658.x · Cited by 27 · see citing works
Saccharomyces cerevisiae positive regulatory gene PET111 encodes a mitochondrial protein that is translated from an mRNA with a long 5' leader.
Strick, C. A., & Fox, T. D. (1987) · Molecular and Cellular Biology · doi:10.1128/mcb.7.8.2728 · Cited by 27 · see citing works
The nucleocytoplasmic conflict, a driving force for the emergence of plant organellar RNA editing
Castandet, B., & Araya, A. (2011) · IUBMB Life · doi:10.1002/iub.581 · Cited by 25 · see citing works
RPM2 , Independently of Its Mitochondrial RNase P Function, Suppresses an ISP42 Mutant Defective in Mitochondrial Import and Is Essential for Normal Growth
Kassenbrock, C. K., Gao, G., Groom, K. R., Sulo, P., Douglas, M. G., & Martín, N. C. R. (1995) · Molecular and Cellular Biology · doi:10.1128/mcb.15.9.4763 · Cited by 25 · see citing works
Contacts between mammalian mitochondrial translational initiation factor 3 and ribosomal proteins in the small subunit
Haque, M. E., Koç, H., Çimen, H., Koc, E. C., & Spremulli, L. L. (2011) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2011.09.013 · Cited by 24 · see citing works
Rpm2p, a Component of Yeast Mitochondrial RNase P, Acts as a Transcriptional Activator in the Nucleus
Stribinskis, V., Heyman, H., Ellis, S. R., Steffen, M. C., & Martín, N. C. R. (2005) · Molecular and Cellular Biology · doi:10.1128/mcb.25.15.6546-6558.2005 · Cited by 24 · see citing works
Yeast AEP3p Is an Accessory Factor in Initiation of Mitochondrial Translation
Lee, C., Tibbetts, A. S., Kramer, G., & Appling, D. R. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.055350 · Cited by 23 · see citing works
Kluyveromyces lactis SEF1 and its Saccharomyces cerevisiae homologue bypass the unknown essential function, but not the mitochondrial RNase P function, of the S. cerevisiae RPM2 gene
Groom, K. R., Heyman, H. C., Steffen, M. C., Hawkins, L., & Martín, N. C. R. (1998) · Yeast · doi:10.1002/(sici)1097-0061(19980115)14:1 · Cited by 18 · see citing works
Rpm2p: separate domains promote tRNA and Rpm1r maturation in Saccharomyces cerevisiae mitochondria
Stribinskis, V. (2001) · Nucleic Acids Research · doi:10.1093/nar/29.17.3631 · Cited by 17 · see citing works
The mature AEP2 gene product of Saccharomyces cerevisiae, required for the expression of subunit 9 of ATP synthase, is a 58 kDa mitochondrial protein
Finnegan, P. M., Tp, E., NAGLEY, P., & Lukins, H. B. (1995) · FEBS Letters · doi:10.1016/0014-5793(95)00727-q · Cited by 15 · see citing works
Two independent activities define Ccm1p as a moonlighting protein in Saccharomyces cerevisiae
Moreno, J. I., Patlolla, B., Belton, K. R., Jenkins, B. C., Radchenkova, P. V., & Piva, M. A. (2012) · Bioscience Reports · doi:10.1042/bsr20120066 · Cited by 13 · see citing works
Suppressor mutations define two regions in the Cbp1 protein important for mitochondrial cytochrome b mRNA stability in Saccharomyces cerevisiae
Islas-Osuna, M. A., Ellis, T. P., Mittelmeier, T. M., & Dieckmann, C. L. (2003) · Current Genetics · doi:10.1007/s00294-003-0405-4 · Cited by 12 · see citing works
Suppressor analyses of temperature-sensitive cbp1 strains of Saccharomyces cerevisiae: the product of the nuclear gene SOC1 affects mitochondrial cytochrome b mRNA post-transcriptionally.
Staples, R. R., & Dieckmann, C. L. (1994) · Genetics · doi:10.1093/genetics/138.3.565 · Cited by 11 · see citing works
Proteasome Mutants, pre4-2 and ump1-2, Suppress the Essential Function but Not the Mitochondrial RNase P Function of the Saccharomyces cerevisiae Gene RPM2
Lutz, M. S., Ellis, S. R., & Martín, N. C. R. (2000) · Genetics · doi:10.1093/genetics/154.3.1013 · Cited by 10 · see citing works
Understanding mitochondrial biogenesis through gene relocation
Sanchirico, M. E. (1998) · ScholarWorks@UMassAmherst (University of Massachusetts Amherst) · Cited by 9 · see citing works
Rise and fall of plant mitochondria
Nick, P. A. (2010) · PROTOPLASMA · doi:10.1007/s00709-010-0139-3 · Cited by 2 · see citing works

Flagged first, then by citations

Sorted by citations

Organization and regulation of mitochondrial protein synthesis
Ott, M., Amunts, A., & Brown, A. (2016) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-060815-014334 · Cited by 282 · see citing works
LRPPRC: A Multifunctional Protein Involved in Energy Metabolism and Human Disease
Cui, J., Wang, L., Ren, X., Zhang, Y., & Zhang, H. (2019) · Frontiers in Physiology · doi:10.3389/fphys.2019.00595 · Cited by 131 · see citing works
Cytochrome c oxidase deficiency
Brischigliaro, M., & Zeviani, M. (2020) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2020.148335 · Cited by 114 · see citing works
Small is big in Arabidopsis mitochondrial ribosome
Waltz, F., Nguyen, T.-T., Arrivé, M., Bochler, A., Chicher, J., Hammann, P., Kühn, L., Quadrado, M., Mireau, H., Hashem, Y., et al. (2019) · Nature Plants · doi:10.1038/s41477-018-0339-y · Cited by 112 · see citing works
Principles of mitoribosomal small subunit assembly in eukaryotes
Harper, N. J., Burnside, C., & Klinge, S. (2022) · Nature · doi:10.1038/s41586-022-05621-0 · Cited by 68 · see citing works
Mitochondrial–nuclear co‐evolution leads to hybrid incompatibility through pentatricopeptide repeat proteins
Jhuang, H., Lee, H., & Leu, J. (2016) · EMBO Reports · doi:10.15252/embr.201643311 · Cited by 57 · see citing works
Modular biogenesis of mitochondrial respiratory complexes
de Barros, M. H., & McStay, G. P. (2019) · Mitochondrion · doi:10.1016/j.mito.2019.10.008 · Cited by 56 · see citing works
Striking Diversity of Mitochondria-Specific Translation Processes across Eukaryotes
Waltz, F., & Giegé, P. (2019) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2019.10.004 · Cited by 43 · see citing works
Mitochondrial genetics revisited
Dujon, B. (2019) · Yeast · doi:10.1002/yea.3445 · Cited by 39 · see citing works
The Schizosaccharomyces pombe PPR protein Ppr10 associates with a novel protein Mpa1 and acts as a mitochondrial translational activator
Wang, Y., Yan, J., Zhang, Q., Ma, X., Zhang, J., Su, M., Wang, X., & Huang, Y. (2017) · Nucleic Acids Research · doi:10.1093/nar/gkx127 · Cited by 34 · see citing works
Starting the engine of the powerhouse: mitochondrial transcription and beyond
Miranda, M., Bonekamp, N. A., & Kühl, I. (2022) · Biological Chemistry · doi:10.1515/hsz-2021-0416 · Cited by 34 · see citing works
The transcriptome of Candida albicans mitochondria and the evolution of organellar transcription units in yeasts
Kolondra, A., Labedzka-Dmoch, K., Wenda, J. M., Drzewicka, K., & Golik, P. (2015) · BMC Genomics · doi:10.1186/s12864-015-2078-z · Cited by 33 · see citing works
Self-citation
Drosophila melanogaster LRPPRC2 is involved in coordination of mitochondrial translation
Baggio, F., Bratić, A. M., Mourier, A., Kauppila, T. E. S., Tain, L. S., Kukat, C., Habermann, B. H., Partridge, L., & Larsson, N. (2014) · Nucleic Acids Research · doi:10.1093/nar/gku1132 · Cited by 30 · see citing works
Drosophila protease ClpXP specifically degrades DmLRPPRC1 controlling mitochondrial mRNA and translation
Matsushima, Y., Hirofuji, Y., Aihara, M., Song, Y., Uchiumi, T., Kaguni, L. S., & Kang, D. (2017) · Scientific Reports · doi:10.1038/s41598-017-08088-6 · Cited by 28 · see citing works
Loss of ppr3, ppr4, ppr6, or ppr10 perturbs iron homeostasis and leads to apoptotic cell death in Schizosaccharomyces pombe
Su, Y., Yang, Y., & Huang, Y. K. (2016) · FEBS Journal · doi:10.1111/febs.13978 · Cited by 22 · see citing works
The pentatricopeptide repeat protein Rmd9 recognizes the dodecameric element in the 3′-UTRs of yeast mitochondrial mRNAs
Hillen, H. S., Markov, D. A., Wojtas, I. D., Hofmann, K. B., Lidschreiber, M., Cowan, A. T., Jones, J. L., Temiakov, D., Cramer, P., & Anikin, M. (2021) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2009329118 · Cited by 21 · see citing works
A restorer‐of‐fertility‐like pentatricopeptide repeat protein promotes cytoplasmic male sterility in Arabidopsis thaliana
Durand, S., Ricou, A., Simon, M., Dehaene, N., Budar, F., & Camilleri, C. (2020) · The Plant Journal · doi:10.1111/tpj.15045 · Cited by 21 · see citing works
The S. pombe mitochondrial transcriptome
Shang, J., Yang, Y., Wu, L., Zou, M., & Huang, Y. K. (2018) · RNA · doi:10.1261/rna.064477.117 · Cited by 19 · see citing works
Yeast mitochondrial protein Pet111p binds directly to two distinct targets in COX2 mRNA, suggesting a mechanism of translational activation
Jones, J. L., Hofmann, K., Cowan, A. T., Temiakov, D., Cramer, P., & Anikin, M. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.ra118.005355 · Cited by 18 · see citing works
Schizosaccharomyces pombe as a fundamental model for research on mitochondrial gene expression: Progress, achievements and outlooks
Dinh, N., & Bonnefoy, N. (2023) · IUBMB Life · doi:10.1002/iub.2801 · Cited by 14 · see citing works
Self-citation
Heterogeneity of the 5′-end in plant mRNA may be involved in mitochondrial translation
Kazama, T., Yagi, Y., Toriyama, K., & Nakamura, T. (2013) · Frontiers in Plant Science · doi:10.3389/fpls.2013.00517 · Cited by 13 · see citing works
Schizosaccharomyces pombe Ppr10 is required for mitochondrial translation
Liu, Z., Li, Y., Xie, W., & Huang, Y. (2020) · FEMS Microbiology Letters · doi:10.1093/femsle/fnaa170 · Cited by 10 · see citing works
Schizosaccharomyces pombe Ppr10 and mpa1 together mediate mitochondrial translational initiation
Luo, Y., Wang, Y., & Huang, Y. (2021) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2021.100869 · Cited by 10 · see citing works
Partial suppression of the respiratory defect of qrs1/her2 glutamyl-tRNA amidotransferase mutants by overexpression of the mitochondrial pentatricopeptide Msc6p
Moda, B. S., Ferreira-Júnior, J. R., & de Barros, M. H. (2016) · Current Genetics · doi:10.1007/s00294-016-0566-6 · Cited by 10 · see citing works
Msc6p is required for mitochondrial translation initiation in the absence of formylated Met‐ tRNA fMet
Franco, L. V. R., Moda, B. S., Soares, M. A. K. M., & de Barros, M. H. (2019) · FEBS Journal · doi:10.1111/febs.14785 · Cited by 9 · see citing works
The FpPPR1 Gene Encodes a Pentatricopeptide Repeat Protein That Is Essential for Asexual Development, Sporulation, and Pathogenesis in Fusarium pseudograminearum
Wang, L., Xie, S., Zhang, Y., Kang, R., Zhang, M., Wang, M., Li, H., Chen, L., Yuan, H., Ding, S., et al. (2021) · Frontiers in Genetics · doi:10.3389/fgene.2020.535622 · Cited by 9 · see citing works
Clingy genes: Why were genes for ribosomal proteins retained in many mitochondrial genomes?
Bertgen, L., Mühlhaus, T., & Herrmann, J. M. (2020) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2020.148275 · Cited by 9 · see citing works
Mitochondrial RNA maturation
Chrzanowska‐Lightowlers, Z. M., & Lightowlers, R. N. (2024) · RNA Biology · doi:10.1080/15476286.2024.2414157 · Cited by 8 · see citing works
Enforcement of Postzygotic Species Boundaries in the Fungal Kingdom
Chou, J., Hsu, P., & Leu, J. (2022) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.00098-22 · Cited by 8 · see citing works
Disruption of ppr3, ppr4, ppr6 or ppr10 induces flocculation and filamentous growth in Schizosaccharomyces pombe
Su, Y., Chen, J., & Huang, Y. K. (2018) · FEMS Microbiology Letters · doi:10.1093/femsle/fny141 · Cited by 7 · see citing works
Translational activators align mRNAs at the small mitoribosomal subunit for translation initiation
Bridgers, J. B., Carlström, A., Sherpa, D., Couvillion, M. T., Rovšnik, U., Gao, J., Wan, B., Shao, S., Ott, M., & Churchman, L. S. (2026) · Nature Structural & Molecular Biology · doi:10.1038/s41594-025-01726-y · Cited by 6 · see citing works
Schizosaccharomyces pombe MAP kinase Sty1 promotes survival of Δppr10 cells with defective mitochondrial protein synthesis
Hu, Y., Luo, Y., Yin, D., Zhao, L., Wang, Y., Yao, R., Zhang, P., Wu, X., Li, M., Hidalgo, E., et al. (2022) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2022.106308 · Cited by 6 · see citing works
More than Just Bread and Wine: Using Yeast to Understand Inherited Cytochrome Oxidase Deficiencies in Humans
Caron-Godon, C. A., Collington, E., Wolf, J. L., Coletta, G., & Glerum, D. M. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25073814 · Cited by 5 · see citing works
Schizosaccharomyces pombe Sls1 is primarily required for cox1 mRNA translation
Wang, Y., Luo, Y., & Huang, Y. K. (2022) · Yeast · doi:10.1002/yea.3813 · Cited by 5 · see citing works
Yeast pentatricopeptide protein Dmr1 (Ccm1) binds a repetitive AU-rich motif in the small subunit mitochondrial ribosomal RNA
Piątkowski, J., & Golik, P. (2020) · RNA · doi:10.1261/rna.074880.120 · Cited by 4 · see citing works
Self-citation
Pentatricopeptide motifs in the N-terminal extension domain of yeast mitochondrial RNA polymerase Rpo41p are not essential for its function
Kruszewski, J., & Golik, P. (2016) · Biochemistry (Moscow) · doi:10.1134/s0006297916100084 · Cited by 4 · see citing works
Self-citation
Mitochondrial mRNA and the small subunit rRNA in budding yeasts undergo 3′-end processing at conserved species-specific elements
Anikin, M., Henry, M. F., Hodorová, V., Houbaviy, H. B., Nosek, J., Pestov, D. G., & Markov, D. A. (2024) · RNA · doi:10.1261/rna.080254.124 · Cited by 3 · see citing works
Requirement of Various Protein Combinations for Each C-to-U RNA Editosome in Plant Organelles
Takenaka, M., Jörg, A., Burger, M., & Haag, S. (2018) · Nucleic acids and molecular biology · doi:10.1007/978-3-319-78190-7_9 · Cited by 3 · see citing works
Candida albicans PPR proteins are required for the expression of respiratory Complex I subunits
Wenda, J. M., Drzewicka, K., Mulica, P., Tetaud, E., di Rago, J. P., Golik, P., & Łabędzka-Dmoch, K. (2024) · GENETICS · doi:10.1093/genetics/iyae124 · Cited by 2 · see citing works
Self-citation
Plant organelle C‐to‐U RNA editing factors can operate successfully in yeast ( Saccharomyces cerevisiae ) as an easily amenable eukaryotic system for their functional analysis
Ramanathan, S., Hanraths, A., Xie, J., Schallenberg‐Rüdinger, M., & Knoop, V. (2025) · FEBS Journal · doi:10.1111/febs.70352 · Cited by 2 · see citing works
Does the study of genetic interactions help predict the function of mitochondrial proteins in Saccharomyces cerevisiae?
Ostojić, J., Glatigny, A., Herbert, C. J., Dujardin, G., & Bonnefoy, N. (2013) · Biochimie · doi:10.1016/j.biochi.2013.11.004 · Cited by 2 · see citing works
Self-citation
Insights into the translational activation mechanisms of the COX1 mRNA in yeast mitochondria
Zamudio‐Ochoa, A., Camacho‐Villasana, Y., Pedroza-Dávila, U., García-Guerrero, A. E., & Pérez-Martı́nez, X. (2025) · Journal of Cell Science · doi:10.1242/jcs.263694 · Cited by 1 · see citing works
Sls1 and Mtf2 mediate the assembly of the Mrh5C complex required for activation of cox1 mRNA translation
Wang, Y., Jin, T., & Huang, Y. K. (2024) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2024.107176 · Cited by 1 · see citing works
The Schizosaccharomyces pombe DEAD-box protein Mss116 is required for mitoribosome assembly and mitochondrial translation
Wang, Y., Feng, G., & Huang, Y. K. (2024) · Mitochondrion · doi:10.1016/j.mito.2024.101881 · Cited by 1 · see citing works
Estudos do gene nuclear MSC6 envolvido na tradução mitocondrial em Saccharomyces cerevisiae
Moda, B. S. (2017) · doi:10.11606/d.87.2017.tde-23012017-141051 · Cited by 1 · see citing works
Neuroendocrine control of vitellogenesisIn the spiny lobster Panulirus homarus(Linnaeus, 1758)
Fernandez, R. (2002) · Eprints@CMFRI Open Access Institutional Repository (Central Marine Fisheries Research Institute)
Research Progress of PPR Protein Family in Plant Growth and Development
沈, 诗. (2023) · International Journal of Ecology · doi:10.12677/ije.2023.122026
The deletion of ppr2 interferes iron sensing and leads to oxidative stress response in Schizosaccharomyces pombe
Liu, Z., Jin, T., Qin, B., Li, R., Shang, J., & Huang, Y. K. (2024) · Mitochondrion · doi:10.1016/j.mito.2024.101875
Transplantation of Saccharomyces cerevisiae Rmd9p peptide into mammalian mitochondrial IF2 substitutes for the IF1 function in Escherichia coli
Singh, J., Sahu, A. K., & Varshney, U. (2026) · Microbiology · doi:10.1099/mic.0.001689
Characterization of the mitochondrial translation apparatus of Arabidopsis thaliana
Waltz, F. (2018) · doi:10.70675/a2a2f5d9z45c7z4e67za4f5z548291e132d1
L’éditosome du chloroplaste : questions, éléments de réponses et digressions
Baudry, K. (2019) · doi:10.70675/039a375dz1167z4ef2z860bze2513b2fb042
Maturation des ARN messagers mitochondriaux et système traductionnel chez l’algue verte Chlamydomonas reinhardtii
Meichel, H. (2023) · doi:10.70675/669245a3z8a42z4953zbaedz2ce6b4472fd5
Orchestration of OXPHOS biogenesis through regulation of mitochondrial translation
Carlström, A., Vazquez‐Calvo, C., & Ott, M. (2026) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2026.120194
Research Progress on the Molecular Regulatory Mechanisms of Non-organellar Localization of PPR Proteins
Li, X., Yan, J., Zhou, L., He, Y., Dong, J., & Zhuang, C. (2026) · Plant Molecular Biology Reporter · doi:10.1007/s11105-026-01751-1

RNA processing, stability and turnover in yeast mitochondria – from genetics to evolution and systems biology
Golik, P. (2010) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2010.04.314
Self-citation
A genome wide study in fission yeast reveals nine PPR proteins that regulate mitochondrial gene expression
Kühl, I., Dujeancourt, L., Gaisne, M., Herbert, C. J., & Bonnefoy, N. (2011) · Nucleic Acids Research · doi:10.1093/nar/gkr511 · Cited by 58 · see citing works
Self-citation
12P.1 Fluorescence in situ hybridization of mitochondrial DNA and RNA
Alán, L., Zelenka, J., Ježek, J., & Ježek, P. (2010) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2010.04.316
Polyadenylation of mt mRNA: Identification of novel deadenylase of human mitochondria
Rorbach, J., Nicholls, T. J. J., & Minczuk, M. A. (2010) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2010.04.317 · Cited by 1 · see citing works
The role of mammalian PPR domain proteins in the regulation of mitochondrial gene expression
Rackham, O., & Filipovska, A. (2011) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2011.10.007 · Cited by 58 · see citing works

Authors: Herbert, C. J., Golik, P., & Bonnefoy, N.
Affiliations: Centre National de la Recherche Scientifique (FR)
Corresponding author: Bonnefoy, Nathalie
ORCID: Bonnefoy, Nathalie
Venue: RNA Biology
Publisher: Informa UK Limited
Published: 2013-09
Volume: 10
Issue: 9
Pages: 1477-1494
ISSN: 1547-6286 (ISSN-L)
1555-8584
DOI: 10.4161/rna.25392
PMC: PMC3858431
OpenAlex: W1975339307
Cited by: 54
References: 105
Citations by year: 2026: 3 · 2025: 3 · 2024: 7 · 2023: 3 · 2022: 5 · 2021: 3 · 2020: 5 · 2019: 8 · 2018: 4 · 2017: 3 · 2016: 5 · 2015: 1 · 2014: 1 · 2013: 2
FWCI: 1.34
Type: journal article
Language: en
Open access: bronze
doi.org
Locations: RNA Biology (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Funders: Centre National de la Recherche Scientifique
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA Research and Splicing
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA and protein synthesis mechanisms
Keywords: PPR proteins, RNA-binding proteins, mitochondrial gene expression, yeast, Saccharomyces cerevisiae, Schizosaccharomyces pombe, mitochondrial membrane
MeSH terms: Computer Simulation, DNA, Mitochondrial, Fungal Proteins, Membrane Proteins, Mitochondria, Schizosaccharomyces, Protein Biosynthesis, Gene Expression Regulation, Fungal, RNA-Binding Proteins, RNA Stability, Mitochondrial Proteins, Saccharomyces cerevisiae Proteins, Ribonuclease P

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review

Yeast PPR proteins, watchdogs of mitochondrial gene expression

Abstract

Integrity signals

Claims the paper makes

Claims other papers make about this one

Self-check

Cites

Cited by

Related

Record

About these checks