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Moonlighting proteins: An intriguing mode of multitasking
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“For example, enolase and glyceraldehyde-3-phosphate dehydrogenase are well-known metabolic enzymes that also act as RNA-binding proteins or surface adhesins in diverse bacterial species (33, 34).”
From Adaptive evolution of Pseudomonas putida in the presence of fluoride exposes novel functions of a benzoate transporter (2026) · cites this paper as [33]
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Function of Mitochondrial Stat3 in Cellular Respiration
Wegrzyn, J., Potla, R., Chwae, Y.-J., Sepuri, N. B. V., Zhang, Q., Koeck, T., Derecka, M., Szczepanek, K., Szelag, M., Gornicka, A., et al. (2009) · Science · doi:10.1126/science.1164551 · Cited by 1,014
Gene duplication and the adaptive evolution of a classic genetic switch
Hittinger, C. T., & Carroll, S. B. (2007) · Nature · doi:10.1038/nature06151 · Cited by 439
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Research works printed but not linked: 83
- Piatigorsky, 1989, Enzyme/crystallins: gene sharing as an evolutionary strategy, Cell, 57, 197, 10.1016/0092-8674(89)90956-2 · DOI
- Hendriks, 1988, Duck lens epsilon-crystallin and lactate dehydrogenase B4 are identical: a single-copy gene product with two distinct functions, Proc. Natl. Acad. Sci. U. S. A., 85, 7114, 10.1073/pnas.85.19.7114 · DOI
- Wistow, 1988, Tau-crystallin/alpha-enolase: one gene encodes both an enzyme and a lens structural protein, J. Cell Biol., 107, 2729, 10.1083/jcb.107.6.2729 · DOI
- Wistow, 1988, Lens crystallins: the evolution and expression of proteins for a highly specialized tissue, Annu. Rev. Biochem., 57, 479, 10.1146/annurev.bi.57.070188.002403 · DOI
- Fujii, 1990, Purification and characterization of rho-crystallin from Japanese common bullfrog lens, J. Biol. Chem., 265, 9914, 10.1016/S0021-9258(19)38759-9 · DOI
- Tomarev, 1992, Characterization of squid crystallin genes. Comparison with mammalian glutathione S-transferase genes, J. Biol. Chem., 267, 8604, 10.1016/S0021-9258(18)42486-6 · DOI
- Zinovieva, 1993, Aldehyde dehydrogenase-derived omega-crystallins of squid and octopus. Specialization for lens expression, J. Biol. Chem., 268, 11449, 10.1016/S0021-9258(18)82144-5 · DOI
- Piatigorsky, 1988, Gene sharing by delta-crystallin and argininosuccinate lyase, Proc. Natl. Acad. Sci. U. S. A., 85, 3479, 10.1073/pnas.85.10.3479 · DOI
- Jeffery, 1999, Moonlighting proteins, Trends Biochem. Sci., 24, 8, 10.1016/S0968-0004(98)01335-8 · DOI · Paper page
- Moore, 2004, Bifunctional and moonlighting enzymes: lighting the way to regulatory control, Trends Plant Sci., 9, 221, 10.1016/j.tplants.2004.03.005 · DOI
- Sriram, 2005, Single-gene disorders: what role could moonlighting enzymes play?, Am. J. Hum. Genet., 76, 911, 10.1086/430799 · DOI
- Gancedo, 2008, Moonlighting proteins in yeasts, Microbiol. Mol. Biol. Rev., 72, 197, 10.1128/MMBR.00036-07 · DOI
- Jeffery, 2004, Molecular mechanisms for multitasking: recent crystal structures of moonlighting proteins, Curr. Opin. Struct. Biol., 14, 663, 10.1016/j.sbi.2004.10.001 · DOI
- Arnér, 2000, Physiological functions of thioredoxin and thioredoxin reductase, Eur. J. Biochem., 267, 6102, 10.1046/j.1432-1327.2000.01701.x · DOI
- Mark, 1976, Escherichia coli thioredoxin: a subunit of bacteriophage T7 DNA polymerase, Proc. Natl. Acad. Sci. U. S. A., 73, 780, 10.1073/pnas.73.3.780 · DOI
- Tabor, 1987, Escherichia coli thioredoxin confers processivity on the DNA polymerase activity of the gene 5 protein of bacteriophage T7, J. Biol. Chem., 262, 16212, 10.1016/S0021-9258(18)47718-6 · DOI
- Bedford, 1997, The thioredoxin binding domain of bacteriophage T7 DNA polymerase confers processivity on Escherichia coli DNA polymerase I, Proc. Natl. Acad. Sci. U. S. A., 94, 479, 10.1073/pnas.94.2.479 · DOI
- Adler, 1983, T7-induced DNA polymerase. Requirement for thioredoxin sulfhydryl groups, J. Biol. Chem., 258, 6956, 10.1016/S0021-9258(18)32317-2 · DOI
- Huber, 1986, Interaction of mutant thioredoxins of Escherichia coli with the gene 5 protein of phage T7. The redox capacity of thioredoxin is not required for stimulation of DNA polymerase activity, J. Biol. Chem., 261, 15006, 10.1016/S0021-9258(18)66820-6 · DOI
- Jitrapakdee, 2008, Structure, mechanism and regulation of pyruvate carboxylase, Biochem. J., 413, 369, 10.1042/BJ20080709 · DOI
- van der Klei, 2006, The significance of peroxisomes in methanol metabolism in methylotrophic yeast, Biochim. Biophys. Acta, 1763, 1453, 10.1016/j.bbamcr.2006.07.016 · DOI
- Ozimek, 2005, Alcohol oxidase: a complex peroxisomal, oligomeric flavoprotein, FEMS Yeast Res., 5, 975, 10.1016/j.femsyr.2005.06.005 · DOI
- Ozimek, 2003, Pyruvate carboxylase is an essential protein in the assembly of yeast peroxisomal oligomeric alcohol oxidase, Mol. Biol. Cell, 14, 786, 10.1091/mbc.E02-07-0417 · DOI
- Ozimek, 2007, The transcarboxylase domain of pyruvate carboxylase is essential for assembly of the peroxisomal flavoenzyme alcohol oxidase, FEMS Yeast Res., 7, 1082, 10.1111/j.1567-1364.2007.00214.x · DOI
- Spasic, 2008, Building gamma-secretase: the bits and pieces, J. Cell Sci., 121, 413, 10.1242/jcs.015255 · DOI
- Fortini, 2009, Notch signaling: the core pathway and its posttranslational regulation, Dev. Cell, 16, 633, 10.1016/j.devcel.2009.03.010 · DOI
- Jacobsen, 2009, Amyloid precursor protein and its homologues: a family of proteolysis-dependent receptors, Cell. Mol. Life Sci., 66, 2299, 10.1007/s00018-009-0020-8 · DOI
- Khandelwal, 2007, Moonlighting activity of presenilin in plants is independent of gamma-secretase and evolutionarily conserved, Proc. Natl. Acad. Sci. U. S. A., 104, 13337, 10.1073/pnas.0702038104 · DOI
- Ow, 2008, Cytochrome c: functions beyond respiration, Nat. Rev. Mol. Cell Biol., 9, 532, 10.1038/nrm2434 · DOI
- Hao, 2005, Specific ablation of the apoptotic functions of cytochrome C reveals a differential requirement for cytochrome C and Apaf-1 in apoptosis, Cell, 121, 579, 10.1016/j.cell.2005.03.016 · DOI
- Kluck, 2000, Determinants of cytochrome c pro-apoptotic activity. The role of lysine 72 trimethylation, J. Biol. Chem., 275, 16127, 10.1074/jbc.275.21.16127 · DOI
- Myers, 2009, Cell biology. Moonlighting in mitochondria, Science, 323, 723, 10.1126/science.1169660 · DOI
- Schindler, 2007, JAK-STAT signaling: from interferons to cytokines, J. Biol. Chem., 282, 20059, 10.1074/jbc.R700016200 · DOI
- Chen, 2005, Aconitase couples metabolic regulation to mitochondrial DNA maintenance, Science, 307, 714, 10.1126/science.1106391 · DOI
- Lu, 2007, Physical interaction between aldolase and vacuolar H+-ATPase is essential for the assembly and activity of the proton pump, J. Biol. Chem., 282, 24495, 10.1074/jbc.M702598200 · DOI
- Yuan, 1997, Glucose-induced microautophagy in Pichia pastoris requires the alpha-subunit of phosphofructokinase, J. Cell Sci., 110, 1935, 10.1242/jcs.110.16.1935 · DOI
- Decker, 2006, Enolase activates homotypic vacuole fusion and protein transport to the vacuole in yeast, J. Biol. Chem., 281, 14523, 10.1074/jbc.M600911200 · DOI
- Kim, 2005, Multifaceted roles of glycolytic enzymes, Trends Biochem. Sci., 30, 142, 10.1016/j.tibs.2005.01.005 · DOI
- Fothergill-Gilmore, 1993, Evolution of glycolysis, Prog. Biophys. Mol. Biol., 59, 105, 10.1016/0079-6107(93)90001-Z · DOI
- Baker, 1991, GCR1 of Saccharomyces cerevisiae encodes a DNA binding protein whose binding is abolished by mutations in the CTTCC sequence motif, Proc. Natl. Acad. Sci. U. S. A., 88, 9443, 10.1073/pnas.88.21.9443 · DOI
- Ozimek, 2006, Hansenula polymorpha and Saccharomyces cerevisiae Pex5p's recognize different, independent peroxisomal targeting signals in alcohol oxidase, FEBS Lett., 580, 46, 10.1016/j.febslet.2005.11.045 · DOI
- Waterham, 1997, Peroxisomal targeting, import, and assembly of alcohol oxidase in Pichia pastoris, J. Cell Biol., 139, 1419, 10.1083/jcb.139.6.1419 · DOI
- Gregory, 2005, Synergy between sequence and size in large-scale genomics, Nat. Rev. Genet., 6, 699, 10.1038/nrg1674 · DOI · Paper page
- Jacob, 1977, Evolution and tinkering, Science, 196, 1161, 10.1126/science.860134 · DOI
- Aharoni, 2005, The ‘evolvability’ of promiscuous protein functions, Nat. Genet., 37, 73, 10.1038/ng1482 · DOI
- Yoshida, 2001, Protein function. Chaperonin turned insect toxin, Nature, 411, 44, 10.1038/35075148 · DOI
- Braig, 1994, The crystal structure of the bacterial chaperonin GroEL at 2.8A, Nature, 371, 578, 10.1038/371578a0 · DOI
- Zhao, 2009, Crystal structure of albaflavenone monooxygenase containing a moonlighting terpene synthase active site, J. Biol. Chem., 284, 36711, 10.1074/jbc.M109.064683 · DOI
- Babady, 2007, Cryptic proteolytic activity of dihydrolipoamide dehydrogenase, Proc. Natl. Acad. Sci. U. S. A., 104, 6158, 10.1073/pnas.0610618104 · DOI
- Chiou, 1991, Ostrich crystallins. Structural characterization of delta-crystallin with enzymic activity, Biochem. J., 273, 295, 10.1042/bj2730295 · DOI
- Rubio-Texeira, 2005, A comparative analysis of the GAL genetic switch between not-so-distant cousins: Saccharomyces cerevisiae versus Kluyveromyces lactis, FEMS Yeast Res., 5, 1115, 10.1016/j.femsyr.2005.05.003 · DOI
- Meyer, 1991, Galactokinase encoded by GAL1 is a bifunctional protein required for induction of the GAL genes in Kluyveromyces lactis and is able to suppress the gal3 phenotype in Saccharomyces cerevisiae, Mol. Cell. Biol., 11, 5454, 10.1128/MCB.11.11.5454 · DOI
- Lohr, 1995, Transcriptional regulation in the yeast GAL gene family: a complex genetic network, FASEB J., 9, 777, 10.1096/fasebj.9.9.7601342 · DOI
- Platt, 2000, The insertion of two amino acids into a transcriptional inducer converts it into a galactokinase, Proc. Natl. Acad. Sci. U. S. A., 97, 3154, 10.1073/pnas.97.7.3154 · DOI
- Bhat, 1992, Overproduction of the GAL1 or GAL3 protein causes galactose-independent activation of the GAL4 protein: evidence for a new model of induction for the yeast GAL/MEL regulon, Mol. Cell. Biol., 12, 2701, 10.1128/MCB.12.6.2701 · DOI
- Sellick, 2009, The effect of ligand binding on the galactokinase activity of yeast Gal1p and its ability to activate transcription, J. Biol. Chem., 284, 229, 10.1074/jbc.M807878200 · DOI
- Klyachko, 2005, pH-dependent substrate preference of pig heart lipoamide dehydrogenase varies with oligomeric state: response to mitochondrial matrix acidification, J. Biol. Chem., 280, 16106, 10.1074/jbc.M414285200 · DOI
- Young, 2008, Confronting the scientific obstacles to global control of tuberculosis, J. Clin. Invest., 118, 1255, 10.1172/JCI34614 · DOI
- Drlica, 1997, DNA gyrase, topoisomerase IV, and the 4-quinolones, Microbiol. Mol. Biol. Rev., 61, 377, 10.1128/.61.3.377-392.1997 · DOI
- Lundqvist, 2007, Exploitation of structural and regulatory diversity in glutamate racemases, Nature, 447, 817, 10.1038/nature05689 · DOI
- Ashiuchi, 2003, Differences in effects on DNA gyrase activity between two glutamate racemases of Bacillus subtilis, the poly-gamma-glutamate synthesis-linking Glr enzyme and the YrpC (MurI) isozyme, FEMS Microbiol. Lett., 223, 221, 10.1016/S0378-1097(03)00381-1 · DOI
- Sengupta, 2006, Glutamate racemase from Mycobacterium tuberculosis inhibits DNA gyrase by affecting its DNA-binding, Nucleic Acids Res., 34, 5567, 10.1093/nar/gkl704 · DOI
- Sengupta, 2008, Moonlighting function of glutamate racemase from Mycobacterium tuberculosis: racemization and DNA gyrase inhibition are two independent activities of the enzyme, Microbiology, 154, 2796, 10.1099/mic.0.2008/020933-0 · DOI
- Podobnik, 2009, A mycobacterial cyclic AMP phosphodiesterase that moonlights as a modifier of cell wall permeability, J. Biol. Chem., 284, 32846, 10.1074/jbc.M109.049635 · DOI
- Pancholi, 1998, alpha-enolase, a novel strong plasmin(ogen) binding protein on the surface of pathogenic streptococci, J. Biol. Chem., 273, 14503, 10.1074/jbc.273.23.14503 · DOI
- Walden, 2006, Structure of dual function iron regulatory protein 1 complexed with ferritin IRE-RNA, Science, 314, 1903, 10.1126/science.1133116 · DOI
- Philpott, 1994, The bifunctional iron-responsive element binding protein/cytosolic aconitase: the role of active-site residues in ligand binding and regulation, Proc. Natl. Acad. Sci. U. S. A., 91, 7321, 10.1073/pnas.91.15.7321 · DOI
- Kennedy, 1992, Purification and characterization of cytosolic aconitase from beef liver and its relationship to the iron-responsive element binding protein, Proc. Natl. Acad. Sci. U. S. A., 89, 11730, 10.1073/pnas.89.24.11730 · DOI
- Banerjee, 2007, Iron-dependent RNA-binding activity of Mycobacterium tuberculosis aconitase, J. Bacteriol., 189, 4046, 10.1128/JB.00026-07 · DOI · Paper page
- Lu, 2001, Interaction between aldolase and vacuolar H+-ATPase: evidence for direct coupling of glycolysis to the ATP-hydrolyzing proton pump, J. Biol. Chem., 276, 30407, 10.1074/jbc.M008768200 · DOI
- Bosch, 2007, Aldolase provides an unusual binding site for thrombospondin-related anonymous protein in the invasion machinery of the malaria parasite, Proc. Natl. Acad. Sci. U. S. A., 104, 7015, 10.1073/pnas.0605301104 · DOI
- Buscaglia, 2003, Sites of interaction between aldolase and thrombospondin-related anonymous protein in plasmodium, Mol. Biol. Cell, 14, 4947, 10.1091/mbc.E03-06-0355 · DOI
- Wang, 1996, The molecular nature of the F-actin binding activity of aldolase revealed with site-directed mutants, J. Biol. Chem., 271, 6861, 10.1074/jbc.271.12.6861 · DOI
- Hall, 2004, Regulation of gene expression by a metabolic enzyme, Science, 306, 482, 10.1126/science.1096773 · DOI
- Jeffery, 2005, Mass spectrometry and the search for moonlighting proteins, Mass Spectrom. Rev., 24, 772, 10.1002/mas.20041 · DOI
- Jeffery, 2009, Moonlighting proteins—an update, Mol. Biosyst., 5, 345, 10.1039/b900658n · DOI
- Bhoumik, 2005, ATM-dependent phosphorylation of ATF2 is required for the DNA damage response, Mol. Cell, 18, 577, 10.1016/j.molcel.2005.04.015 · DOI
- Hu, 2009, Profiling the human protein–DNA interactome reveals ERK2 as a transcriptional repressor of interferon signaling, Cell, 139, 610, 10.1016/j.cell.2009.08.037 · DOI
- Irion, 2007, bicoid RNA localization requires specific binding of an endosomal sorting complex, Nature, 445, 554, 10.1038/nature05503 · DOI
- Moore, 2003, Role of the Arabidopsis glucose sensor HXK1 in nutrient, light, and hormonal signaling, Science, 300, 332, 10.1126/science.1080585 · DOI
- Entelis, 2006, A glycolytic enzyme, enolase, is recruited as a cofactor of tRNA targeting toward mitochondria in Saccharomyces cerevisiae, Genes Dev., 20, 1609, 10.1101/gad.385706 · DOI
- Ruiz, 2009, Moonlighting proteins Hal3 and Vhs3 form a heteromeric PPCDC with Ykl088w in yeast CoA biosynthesis, Nat. Chem. Biol., 5, 920, 10.1038/nchembio.243 · DOI
- Kaufman, 2003, A function for the mitochondrial chaperonin Hsp60 in the structure and transmission of mitochondrial DNA nucleoids in Saccharomyces cerevisiae, J. Cell Biol., 163, 457, 10.1083/jcb.200306132 · DOI
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Metadata
- Authors
- Huberts, D. H. E. W., & van der Klei, I. J.
- Venue
- Biochimica et Biophysica Acta (BBA) - Molecular Cell Research
- Publisher
- Elsevier BV
- Published
- 2010-04
- Volume
- 1803
- Issue
- 4
- Pages
- 520-525
- ISSN
- 0167-4889
- Cited by
- 405
- References
- 2
- Language
- en
- Licence
- Funders
- Division of Chemical Sciences of The Netherlands Organisation for Scientific Research (NWO-CW)
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