ArticleJournal of molecular biology2011
Structure of H/ACA RNP protein Nhp2p reveals cis/trans isomerization of a conserved proline at the RNA and Nop10 binding interface.
Article in Journal of molecular biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 34 citations in OpenAlex.
- Intrinsically disordered regions are not sufficient to direct the compartmental localization of nucleolar proteins in the nucleus.PLoS biology · 2023Article
- Novel pathological variants of NHP2 affect N-terminal domain flexibility, protein stability, H/ACA Ribonucleoprotein (RNP) complex formation and telomerase activity.Human molecular genetics · 2023Article
- New Insights into Dyskerin-CypA Interaction: Implications for X-Linked Dyskeratosis Congenita and Beyond.Genes · 2023Article
- Eukaryote specific RNA and protein features facilitate assembly and catalysis of H/ACA snoRNPs.Nucleic acids research · 2021Article
- Pseudouridylation defect due toProceedings of the National Academy of Sciences of the United States of America · 2020Article
- Structural Biology of Telomerase.Cold Spring Harbor perspectives in biology · 2019Review
- Improving mass spectrometry analysis of protein structures with arginine-selective chemical cross-linkers.Nature communications · 2019Article
- Biology and clinical relevance of noncoding sno/scaRNAs.Trends in cardiovascular medicine · 2018Review
- Progress in Human and Tetrahymena Telomerase Structure Determination.Annual review of biophysics · 2017Review
- Human intron-encoded AluACA RNAs and telomerase RNA share a common element promoting RNA accumulation.RNA biology · 2016Article
- Progress in structural studies of telomerase.Current opinion in structural biology · 2014Review
- Article
- Telomeres at a glance.Journal of cell science · 2012Review
- Human intron-encoded Alu RNAs are processed and packaged into Wdr79-associated nucleoplasmic box H/ACA RNPs.Genes & development · 2012Article
- An enhanced H/ACA RNP assembly mechanism for human telomerase RNA.Molecular and cellular biology · 2012Article
- YbxF and YlxQ are bacterial homologs of L7Ae and bind K-turns but not K-loops.RNA (New York, N.Y.) · 2012Article
- Structure of the interleukin-2 tyrosine kinase Src homology 2 domain; comparison between X-ray and NMR-derived structures.Acta crystallographica. Section F, Structural biology and crystallization communications · 2012Article
- Architecture of human telomerase RNA.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
- Reconstitution and structural analysis of the yeast box H/ACA RNA-guided pseudouridine synthase.Genes & development · 2011Article
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7 authors at 1 institution in 1 country.
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Abstract
H/ACA small nucleolar and Cajal body ribonucleoproteins (RNPs) function in site-specific pseudouridylation of eukaryotic rRNA and snRNA, rRNA processing, and vertebrate telomerase biogenesis. Nhp2, one of four essential protein components of eukaryotic H/ACA RNPs, forms a core trimer with the pseudouridylase Cbf5 and Nop10 that binds to H/ACA RNAs specifically. Crystal structures of archaeal H/ACA RNPs have revealed how the protein components interact with each other and with the H/ACA RNA. However, in place of Nhp2p, archaeal H/ACA RNPs contain L7Ae, which binds specifically to an RNA K-loop motif absent from eukaryotic H/ACA RNPs, while Nhp2 binds a broader range of RNA structures. We report solution NMR studies of Saccharomyces cerevisiae Nhp2 (Nhp2p), which reveal that Nhp2p exhibits two major conformations in solution due to cis/trans isomerization of the evolutionarily conserved Pro83. The equivalent proline is in the cis conformation in all reported structures of L7Ae and other homologous proteins. Nhp2p has the expected α-β-α fold, but the solution structures of the major conformation of Nhp2p with trans Pro83 and of Nhp2p-S82W with cis Pro83 reveal that Pro83 cis/trans isomerization affects the positions of numerous residues at the Nop10 and RNA binding interface. An S82W substitution, which stabilizes the cis conformation, also stabilizes the association of Nhp2p with H/ACA snoRNPs expressed in vivo. We propose that Pro83 plays a key role in the assembly of the eukaryotic H/ACA RNP, with the cis conformation locking in a stable Cbf5-Nop10-Nhp2 ternary complex and positioning the protein backbone to interact with the H/ACA RNA.
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