ArticleJournal of molecular biology2009
The box H/ACA snoRNP assembly factor Shq1p is a chaperone protein homologous to Hsp90 cochaperones that binds to the Cbf5p enzyme.
Article in Journal of molecular biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
16 citing papers in PubMed, 22 citations in OpenAlex.
- Small Nucleolar RNAs (snoRNAs) in Cancer: From Biogenesis to Clinical Potential.OncoTargets and therapy · 2026Review
- The Role of Hsp90-R2TP in Macromolecular Complex Assembly and Stabilization.Biomolecules · 2022Review
- H/ACA Small Ribonucleoproteins: Structural and Functional Comparison Between Archaea and Eukaryotes.Frontiers in microbiology · 2021Review
- Efficient RNA pseudouridylation by eukaryotic H/ACA ribonucleoproteins requires high affinity binding and correct positioning of guide RNA.Nucleic acids research · 2018Article
- Assembly and trafficking of box C/D and H/ACA snoRNPs.RNA biology · 2017Review
- Placeholder factors in ribosome biogenesis: please, pave my way.Microbial cell (Graz, Austria) · 2017Review
- Structure of GPN-Loop GTPase Npa3 and Implications for RNA Polymerase II Assembly.Molecular and cellular biology · 2015Article
- Structure and interactions of the CS domain of human H/ACA RNP assembly protein Shq1.Journal of molecular biology · 2015Article
- RNA-guided isomerization of uridine to pseudouridine--pseudouridylation.RNA biology · 2014Review
- Mechanism of the AAA+ ATPases pontin and reptin in the biogenesis of H/ACA RNPs.RNA (New York, N.Y.) · 2012Article
- Biology and applications of small nucleolar RNAs.Cellular and molecular life sciences : CMLS · 2011Review
- Structure of the Shq1-Cbf5-Nop10-Gar1 complex and implications for H/ACA RNP biogenesis and dyskeratosis congenita.The EMBO journal · 2011Article
- The H/ACA RNP assembly factor SHQ1 functions as an RNA mimic.Genes & development · 2011Article
- Structures of ribonucleoprotein particle modification enzymes.Quarterly reviews of biophysics · 2011Review
- Article
- Identification and characterization of GRIM-1, a cell-death-associated gene product.Journal of cell science · 2010Article
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 2 countries.
Funding
Abstract
Box H/ACA small nucleolar (sno) ribonucleoproteins (RNPs) are responsible for the formation of pseudouridine in a variety of RNAs and are essential for ribosome biogenesis, modification of spliceosomal RNAs, and telomerase stability. A mature snoRNP has been reconstituted in vitro and is composed of a single RNA and four proteins. However, snoRNP biogenesis in vivo requires multiple factors to coordinate a complex and poorly understood assembly and maturation process. Among the factors required for snoRNP biogenesis in yeast is Shq1p, an essential protein necessary for stable expression of box H/ACA snoRNAs. We have found that Shq1p consists of two independent domains that contain casein kinase 1 phosphorylation sites. We also demonstrate that Shq1p binds the pseudourydilating enzyme Cbf5p through the C-terminal domain, in synergy with the N-terminal domain. The NMR solution structure of the N-terminal domain has striking homology to the 'Chord and Sgt1' domain of known Hsp90 cochaperones, yet Shq1p does not interact with the yeast Hsp90 homologue in vitro. Surprisingly, Shq1p has stand-alone chaperone activity in vitro. This activity is harbored by the C-terminal domain, but it is increased by the presence of the N-terminal domain. These results provide the first evidence of a specific biochemical activity for Shq1p and a direct link to the H/ACA snoRNP.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.