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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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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