Cited by 199RNA modifications and cancerRNA and protein synthesis mechanismsNuclear Structure and Function

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Architecture and assembly of mammalian H/ACA small nucleolar and telomerase ribonucleoproteins

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Wang, Chen, Meier, U Thomas·2004·The EMBO Journal

DOI 10.1038/sj.emboj.7600181PMC PMC394235

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Abstract

Mammalian H/ACA small nucleolar RNAs and telomerase RNA share common sequence and secondary structure motifs that form ribonucleoprotein particles (RNPs) with the same four core proteins, NAP57 (also dyskerin or in yeast Cbf5p), GAR1, NHP2, and NOP10. The assembly and molecular interactions of the components of H/ACA RNPs are unknown. Using in vitro transcription/translation in combination with immunoprecipitation of core proteins, UV-crosslinking, and electrophoretic mobility shift assays, we demonstrate the following. NOP10 associates with NAP57 as a prerequisite for NHP2 binding. Although NHP2 on its own binds RNA nonspecifically, this NAP57-NOP10-NHP2 core trimer specifically recognizes H/ACA RNAs. GAR1 associates independently with NAP57 near the pseudouridylase core of mature H/ACA RNPs. In contrast to other RNPs whose assembly is initiated by protein-RNA interactions, the four H/ACA core proteins form a protein-only particle that associates with H/ACA RNAs. Nonetheless, functional H/ACA snoRNPs assembled in cytosolic extracts are stable and do not exchange their RNA components, suggesting that new particle formation requires de novo synthesis.

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Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa.
Schägger, H., & von Jagow, G. (1987) · Analytical Biochemistry · doi:10.1016/0003-2697(87)90587-2 · Cited by 11,420
Accurate transcription initiation by RNA polymerase II in a soluble extract from isolated mammalian nuclei
Dignam, J. D., Lebovitz, R. M., & Roeder, R. G. (1983) · Nucleic Acids Research · doi:10.1093/nar/11.5.1475 · Cited by 11,262
The RNA Component of Human Telomerase
Feng, J., Funk, W. D., Wang, S.-S., Weinrich, S. L., Avilion, A. A., Chiu, C.-P., Adams, R. R., Chang, E., Allsopp, R. C., Yu, J., et al. (1995) · Science · doi:10.1126/science.7544491 · Cited by 2,227
Eukaryotic proteins expressed in Escherichia coli: an improved thrombin cleavage and purification procedure of fusion proteins with glutathione S-transferase.
Guan, K., & Dixon, J. (1991) · Analytical Biochemistry · doi:10.1016/0003-2697(91)90534-z · Cited by 1,735
A telomerase component is defective in the human disease dyskeratosis congenita
Mitchell, J. R., Wood, E., & Collins, K. (1999) · Nature · doi:10.1038/990141 · Cited by 1,168
X-linked dyskeratosis congenita is caused by mutations in a highly conserved gene with putative nucleolar functions
Heiss, N. S., Knight, S. W., Vulliamy, T. J., Klauck, S. M., Wiemann, S., Mason, P. J., Poustka, A., & Dokal, I. (1998) · Nature Genetics · doi:10.1038/ng0598-32 · Cited by 976
Site-Specific Pseudouridine Formation in Preribosomal RNA Is Guided by Small Nucleolar RNAs
Ganot, P., Bortolin‐Cavaillé, M., & Kiss, T. (1997) · Cell · doi:10.1016/s0092-8674(00)80263-9 · Cited by 643
Small Nucleolar RNAs Direct Site-Specific Synthesis of Pseudouridine in Ribosomal RNA
Ni, J., Tien, A. L., & Fournier, M. J. (1997) · Cell · doi:10.1016/s0092-8674(00)80238-x · Cited by 519
Interactions between small nuclear ribonucleoprotein particles in formation of spliceosomes
Konarska, M. M., & Sharp, P. A. (1987) · Cell · doi:10.1016/0092-8674(87)90614-3 · Cited by 516
A Box H/ACA Small Nucleolar RNA-Like Domain at the Human Telomerase RNA 3′ End
Mitchell, J. R., Cheng, J., & Collins, K. (1999) · Molecular and Cellular Biology · doi:10.1128/mcb.19.1.567 · Cited by 510
Function and synthesis of small nucleolar RNAs
Tollervey, D. W., & Kiss, T. (1997) · Current Opinion in Cell Biology · doi:10.1016/s0955-0674(97)80005-1 · Cited by 467
Dyskeratosis Congenita and Cancer in Mice Deficient in Ribosomal RNA Modification
Ruggero, D., Grisendi, S., Piazza, F., Rego, E. M., Mari, F., Rao, P. H., Cordon‐Cardo, C., & Pandolfi, P. P. (2003) · Science · doi:10.1126/science.1079447 · Cited by 450
Nopp 140 shuttles on tracks between nucleolus and cytoplasm
Meier, U. T., & Blobel, G. (1992) · Cell · doi:10.1016/0092-8674(92)90539-o · Cited by 417
Self-citation
The box H + ACA snoRNAs carry Cbf5p, the putative rRNA pseudouridine synthase.Preprint
Lafontaine, D., Bousquet-Antonelli, C., Henry, Y., Caizergues-Ferrer, M., & Tollervey, D. (1998) · Genes & Development · doi:10.1101/gad.12.4.527 · Cited by 371
Identification of 86 candidates for small non-messenger RNAs from the archaeon Archaeoglobus fulgidus
Tang, T., Bachellerie, J., Rozhdestvensky, T. S., Bortolin‐Cavaillé, M., Huber, H., Drungowski, M., Elge, T., Brosius, J., & Hüttenhofer, A. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.112047299 · Cited by 337
A Common Core RNP Structure Shared between the Small Nucleoar Box C/D RNPs and the Spliceosomal U4 snRNP
Watkins, N. J., Senty-Segault, V., Charpentier, B., Nottrott, S., Fabrizio, P., Bachi, A., Wilm, M. S., Rosbash, M., Branlant, C., & Lührmann, R. (2000) · Cell · doi:10.1016/s0092-8674(00)00137-9 · Cited by 331
Sno Storm in the Nucleolus: New Roles for Myriad Small RNPs
Smith, C. M., & STEITZ, J. A. (1997) · Cell · doi:10.1016/s0092-8674(00)80247-0 · Cited by 313
Ribosome Structure and Activity Are Altered in Cells Lacking snoRNPs that Form Pseudouridines in the Peptidyl Transferase Center
King, T. H., Liu, B., McCully, R. R., & Fournier, M. J. (2003) · Molecular Cell · doi:10.1016/s1097-2765(03)00040-6 · Cited by 292
Cocrystal Structure of a tRNA Ψ55 Pseudouridine Synthase
Hoang, C., & Ferré-D’Amaré, A. R. (2001) · Cell · doi:10.1016/s0092-8674(01)00618-3 · Cited by 287
GAR1 is an essential small nucleolar RNP protein required for pre‐rRNA processing in yeast.
Girard, J., Lehtonen, H., Caizergues‐Ferrer, M., Amalric, F., Tollervey, D. W., & Lapeyre, B. (1992) · The EMBO Journal · doi:10.1002/j.1460-2075.1992.tb05099.x · Cited by 276
In Vivo Analysis of Cajal Body Movement, Separation, and Joining in Live Human Cells
Platani, M., Goldberg, I., Swedlow, J. R., & Lamond, A. I. (2000) · The Journal of Cell Biology · doi:10.1083/jcb.151.7.1561 · Cited by 275
NAP57, a mammalian nucleolar protein with a putative homolog in yeast and bacteria.
Meier, U. T., & Blobel, G. (1994) · The Journal of Cell Biology · doi:10.1083/jcb.127.6.1505 · Cited by 258
Self-citation
Modifications of U2 snRNA are required for snRNP assembly and pre‐mRNA splicing
Yu, Y., Shu, M., & Steitz, J. A. (1998) · The EMBO Journal · doi:10.1093/emboj/17.19.5783 · Cited by 251
Nhp2p and Nop10p are essential for the function of H/ACA snoRNPs
Henras, A. K., Henry, Y. A. L., Bousquet‐Antonelli, C., Noaillac‐Depeyre, J., Gélugne, J., & Caizergues‐Ferrer, M. (1998) · The EMBO Journal · doi:10.1093/emboj/17.23.7078 · Cited by 247
Identification and characterization of a yeast nucleolar protein that is similar to a rat liver nucleolar protein.
Aris, J. P., & Blobel, G. (1988) · The Journal of Cell Biology · doi:10.1083/jcb.107.1.17 · Cited by 237
Human H/ACA Small Nucleolar RNPs and Telomerase Share Evolutionarily Conserved Proteins NHP2 and NOP10
Pogačić, V., Dragon, F., & Filipowicz, W. (2000) · Molecular and Cellular Biology · doi:10.1128/mcb.20.23.9028-9040.2000 · Cited by 232
Unexplained aplastic anaemia, immunodeficiency, and cerebellar hypoplasia (Hoyeraal‐Hreidarsson syndrome) due to mutations in the dyskeratosis congenita gene, DKC1
Knight, S. W., Heiss, N. S., Vulliamy, T., Aalfs, C. M., McMahon, C., Richmond, P., Jones, A., Hennekam, R. C. M., Poustka, A., Mason, P. J., et al. (1999) · British Journal of Haematology · doi:10.1046/j.1365-2141.1999.01690.x · Cited by 232
Point Mutations in Yeast CBF5 Can Abolish In Vivo Pseudouridylation of rRNA
Zebarjadian, Y., King, T., Fournier, M. J., Clarke, L., & Carbon, J. A. (1999) · Molecular and Cellular Biology · doi:10.1128/mcb.19.11.7461 · Cited by 224
RNA-guided Nucleotide Modification of Ribosomal and Other RNAs
Decatur, W. A., & Fournier, M. J. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.r200023200 · Cited by 214
Binding of L7Ae protein to the K-turn of archaeal snoRNAs: a shared RNA binding motif for C/D and H/ACA box snoRNAs in Archaea
Rozhdestvensky, T. S. (2003) · Nucleic Acids Research · doi:10.1093/nar/gkg175 · Cited by 214
Cbf5p, a potential pseudouridine synthase, and Nhp2p, a putative RNA-binding protein, are present together with Gar1p in all H BOX/ACA-motif snoRNPs and constitute a common bipartite structure
Watkins, N. J., GOTTSCHALK, A. R., Neubauer, G., Kastner, B., Fabrizio, P., Mann, M., & Lührmann, R. (1998) · RNA · doi:10.1017/s1355838298980761 · Cited by 214
She2p is a novel RNA‐binding protein that recruits the Myo4p–She3p complex to ASH1 mRNA
Long, R. M., Gu, W., Lorimer, E., Singer, R. H., & Chartrand, P. (2000) · The EMBO Journal · doi:10.1093/emboj/19.23.6592 · Cited by 212
Structural elements required for the localization of ASH1 mRNA and of a green fluorescent protein reporter particle in vivo
Chartrand, P., Meng, X.-H., Singer, R. H., & Long, R. M. (1999) · Current Biology · doi:10.1016/s0960-9822(99)80144-4 · Cited by 209
Novel Predicted RNA-Binding Domains Associated with the Translation Machinery
Aravind, L., & Koonin, E. V. (1999) · Journal of Molecular Evolution · doi:10.1007/pl00006472 · Cited by 193
Functional interaction of a novel 15.5kD[U4/U6·U5] tri‐snRNP protein with the5′ stem–loop of U4 snRNA
Nottrott, S., Hartmuth, K., Fabrizio, P., Urlaub, H., Vidovic, I., Ficner, R., & Lührmann, R. (1999) · The EMBO Journal · doi:10.1093/emboj/18.21.6119 · Cited by 184
In Vitro Assembly of Human H/ACA Small Nucleolar RNPs Reveals Unique Features of U17 and Telomerase RNAs
Dragon, F., Pogačić, V., & Filipowicz, W. (2000) · Molecular and Cellular Biology · doi:10.1128/mcb.20.9.3037-3048.2000 · Cited by 171
Guiding ribose methylation of rRNA
Bachellerie, J., & Cavaillé, J. (1997) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(97)01057-8 · Cited by 170
An Essential Yeast Protein, CBF5p, Binds In Vitro to Centromeres and Microtubules
Jiang, W., Middleton, K. M., Yoon, H.-J., Fouquet, C., & Carbon, J. A. (1993) · Molecular and Cellular Biology · doi:10.1128/mcb.13.8.4884 · Cited by 163
A small nucleolar RNP protein is required for pseudouridylation of eukaryotic ribosomal RNAs
Bousquet‐Antonelli, C., Henry, Y. A. L., Gélugne, J., Caizergues‐Ferrer, M., & Kiss, T. (1997) · The EMBO Journal · doi:10.1093/emboj/16.15.4770 · Cited by 150
A Conserved Aspartate of tRNA Pseudouridine Synthase Is Essential for Activity and a Probable Nucleophilic Catalyst
Huang, L., Pookanjanatavip, M., Gu, X., & Santi, D. V. (1998) · Biochemistry · doi:10.1021/bi971874+ · Cited by 147
Purification, cloning, and properties of the tRNA psi 55 synthase from Escherichia coli.
Nurse, K., Wrzesiński, J., Bakin, A. V., Lane, B. G., & Ofengand, J. (1995) · PubMed Central · Cited by 132
Elements essential for accumulation and function of small nucleolar RNAs directing site‐specific pseudouridylation of ribosomal RNAs
Bortolin‐Cavaillé, M., Ganot, P., & Kiss, T. (1999) · The EMBO Journal · doi:10.1093/emboj/18.2.457 · Cited by 126
Site‐specific cross‐linking analyses reveal an asymmetric protein distribution for a box C/D snoRNP
Cahill, N. M., Friend, K., Speckmann, W. A., Li, Z., Terns, R. M., Terns, M. P., & STEITZ, J. A. (2002) · The EMBO Journal · doi:10.1093/emboj/cdf376 · Cited by 112
Exclusive Interaction of the 15.5 kD Protein with the Terminal Box C/D Motif of a Methylation Guide snoRNP
Weinstein, L. B., DeGregorio, S. J., Strobel, S. A., & STEITZ, J. A. (2002) · Chemistry & Biology · doi:10.1016/s1074-5521(02)00239-9 · Cited by 110
A Well-Connected and Conserved Nucleoplasmic Helicase Is Required for Production of Box C/D and H/ACA snoRNAs and Localization of snoRNP Proteins
King, T. H., Decatur, W. A., Bertrand, É., Maxwell, E. S., & Fournier, M. J. (2001) · Molecular and Cellular Biology · doi:10.1128/mcb.21.22.7731-7746.2001 · Cited by 110
The mechanism of pseudouridine synthase I as deduced from its interaction with 5-fluorouracil-tRNA
Gu, X., Liu, Y., & Santi, D. V. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.25.14270 · Cited by 106
Dyskeratosis congenita: its link to telomerase and aplastic anaemia
Dokal, I. S., & Vulliamy, T. (2003) · Blood Reviews · doi:10.1016/s0268-960x(03)00020-1 · Cited by 100
Evolutionary appearance of genes encoding proteins associated with box H/ACA snoRNAs: Cbf5p in Euglena gracilis, an early diverging eukaryote, and candidate Gar1p and Nop10p homologs in archaebacteria
Watanabe, Y. (2000) · Nucleic Acids Research · doi:10.1093/nar/28.12.2342 · Cited by 93
Comparison of the Rat Nucleolar Protein Nopp140 with Its Yeast Homolog SRP40
Meier, U. T. (1996) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)84375-2 · Cited by 91
Self-citation
Naf1p is a box H/ACA snoRNP assembly factor
Fatica, A., Dlakić, M., & Tollervey, D. W. (2002) · RNA · doi:10.1017/s1355838202022094 · Cited by 88
Stable expression in yeast of the mature form of human telomerase RNA depends on its association with the box H/ACA small nucleolar RNP proteins Cbf5p, Nhp2p and Nop10p
Dez, C. (2001) · Nucleic Acids Research · doi:10.1093/nar/29.3.598 · Cited by 81
Immunopurified Small Nucleolar Ribonucleoprotein Particles Pseudouridylate rRNA Independently of Their Association with Phosphorylated Nopp140
Wang, C., Query, C. C., & Meier, U. T. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.22.24.8457-8466.2002 · Cited by 80
Self-citation
Accumulation of H/ACA snoRNPs depends on the integrity of the conserved central domain of the RNA-binding protein Nhp2p
Henras, A. K. (2001) · Nucleic Acids Research · doi:10.1093/nar/29.13.2733 · Cited by 77
Human Genome and Diseases:�Dyskeratosis congenita
Marrone, A., & Mason, P. J. (2003) · Cellular and Molecular Life Sciences · doi:10.1007/s000180300042 · Cited by 76
The Shq1p·Naf1p Complex Is Required for Box H/ACA Small Nucleolar Ribonucleoprotein Particle Biogenesis
Yang, P. K., Rotondo, G., Porras, T., Legrain, P., & Chanfreau, G. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m207669200 · Cited by 74
Dyskerin Localizes to the Nucleolus and Its Mislocalization Is Unlikely to Play a Role in the Pathogenesis of Dyskeratosis Congenita
Heiss, N. S., Girod, A., Salowsky, R., Wiemann, S., Pepperkok, R., & Poustka, A. J. (1999) · Human Molecular Genetics · doi:10.1093/hmg/8.13.2515 · Cited by 73
Naf1p, an Essential Nucleoplasmic Factor Specifically Required for Accumulation of Box H/ACA Small Nucleolar RNPs
Dez, C., Noaillac‐Depeyre, J., Caizergues‐Ferrer, M., & Henry, Y. A. L. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.22.20.7053-7065.2002 · Cited by 64
Gar1p Binds to the Small Nucleolar RNAs snR10 and snR30 in Vitro through a Nontypical RNA Binding Element
Bagni, C., & Lapeyre, B. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.18.10868 · Cited by 58
Functional Redundancy of Spb1p and a snR52-Dependent Mechanism for the 2′-O-Ribose Methylation of a Conserved rRNA Position in Yeast
Bonnerot, C., Pintard, L., & Lutfalla, G. (2003) · Molecular Cell · doi:10.1016/s1097-2765(03)00435-0 · Cited by 56
Isolation and Characterization of the Small Nucleolar Ribonucleoprotein Particle snR30 from Saccharomyces cerevisiae
Lübben, B., Fabrizio, P., Kastner, B., & Lührmann, R. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.19.11549 · Cited by 55
An Essential Yeast Protein, CBF5p, Binds In Vitro to Centromeres and Microtubules
Jiang, W., Middleton, K. M., Yoon, H., et al. (1993) · Molecular and Cellular Biology · doi:10.1128/mcb.13.8.4884-4893.1993 · Cited by 53
In vivo analysis of nucleolar proteins modified by the yeast arginine methyltransferase Hmt1/Rmt1p
Xu, C., Henry, P. A., Setya, A., & Henry, M. F. (2003) · RNA · doi:10.1261/rna.5020803 · Cited by 49
Identification of the First Trypanosome H/ACA RNA That Guides Pseudouridine Formation on rRNA
Liang, X., Liu, L., & Michaeli, S. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m104488200 · Cited by 47
Identification of a segment of the small nucleolar ribonucleoprotein-associated protein GAR1 that is sufficient for nucleolar accumulation
Girard, J., Bagni, C., Caizergues‐Ferrer, M., Amalric, F., & Lapeyre, B. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)32337-2 · Cited by 43
RNase Treatment of Yeast and Mammalian Cell Extracts Affects in Vitro Substrate Methylation by Type I Protein Arginine N-Methyltransferases
Frankel, A., & Clarke, S. G. (1999) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1999.0779 · Cited by 41
A Physical Interaction between Gar1p and Rnt1p Is Required for the Nuclear Import of H/ACA Small Nucleolar RNA-Associated Proteins
Tremblay, A., Lamontagne, B., Catala, M., Yam, Y., Larose, S., Good, L., & Elela, S. A. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.22.13.4792-4802.2002 · Cited by 25
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Youssoufian, H., Gharibyan, V., & Qatanani, M. (1999) · Blood Cells Molecules and Diseases · doi:10.1006/bcmd.1999.0258 · Cited by 18

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Authors: Wang, C., & Meier, U. T.
Affiliations: Albert Einstein College of Medicine (US)
Corresponding author: Meier, U Thomas
ORCID: Wang, Chen
Meier, U Thomas
Venue: The EMBO Journal
Publisher: Springer Science and Business Media LLC
Published: 2004-03-25
Volume: 23
Issue: 8
Pages: 1857-1867
ISSN: 0261-4189 (ISSN-L)
1460-2075
DOI: 10.1038/sj.emboj.7600181
PMC: PMC394235
OpenAlex: W2122834552
Cited by: 199
References: 67
Citations by year: 2026: 2 · 2025: 3 · 2024: 2 · 2023: 12 · 2022: 6 · 2021: 19 · 2020: 4 · 2019: 7 · 2018: 6 · 2017: 4 · 2016: 10 · 2015: 7 · 2014: 7 · 2013: 9 · 2012: 11
FWCI: 6.41
Type: journal article
Language: en
Open access: bronze
doi.org
Licence: www.springernature.com/gp/researchers/text-and-data-mining (tdm)
www.springernature.com/gp/researchers/text-and-data-mining (vor)
Locations: The EMBO Journal (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Funders: American Cancer Society
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA modifications and cancer
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA and protein synthesis mechanisms
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Nuclear Structure and Function
Keywords: telomerase RNA, ribonucleoprotein assembly, dyskerin, NOP10, NHP2, GAR1, RNA-protein interactions, RNA recognition, snoRNA processing, telomerase
MeSH terms: Animals, Cell Extracts, Humans, Mammals, Mutation, Nuclear Proteins, Protein Binding, RNA, Ultraviolet Rays, Uridine, RNA-Binding Proteins, Ribonucleoproteins, Small Nuclear, Telomerase, RNA, Small Nucleolar, Ribonucleoproteins, Small Nucleolar, Rats

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Architecture and assembly of mammalian H/ACA small nucleolar and telomerase ribonucleoproteins

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