Evidence map›Paper›PMID 25553844›Full record

ArticleJournal of molecular biology2015

Structure and interactions of the CS domain of human H/ACA RNP assembly protein Shq1.

Mahavir Singh, Zhonghua Wang, Duilio Cascio, Juli Feigon

Open access · greenAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Journal of molecular biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
0.4field-weighted citation impact, top 36% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

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.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

8 citing papers in PubMed, 12 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Article
  5. Crystal structures of the naturally fused CS and cytochrome bActa crystallographica. Section D, Structural biology · 2019
    Article
  6. Article
  7. Review
  8. Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

4 authors at 1 institution in 1 country.

Mahavir SinghDepartment of Chemistry and Biochemistry, University of California, Los Angeles, CA 90095, USA.
Zhonghua WangDepartment of Chemistry and Biochemistry, University of California, Los Angeles, CA 90095, USA.
Duilio CascioUniversity of California Los Angeles-Department of Energy (UCLA-DOE) Institute for Genomics and Proteomics, University of California, Los Angeles, CA 90095, USA.
Juli FeigonDepartment of Chemistry and Biochemistry, University of California, Los Angeles, CA 90095, USA; University of California Los Angeles-Department of Energy (UCLA-DOE) Institute for Genomics and Proteomics, University of California, Los Angeles, CA 90095, USA. Electronic address: feigon@mbi.ucla.edu.
University of California, Los Angeles · US

Funding

Y-FAMILY POLYMERASES AND CO-FACTORS IN TRANSLESION REPLICATIONP41RR015301 · NCRR · CORNELL UNIVERSITY ITHACA · PI DONG, ZIGANG · 2001 to 2011
$28.2M
Overall EvaluationP41GM103403 · NIGMS · CORNELL UNIVERSITY · PI EALICK, STEVEN E · 2012 to 2017
$14.3M
STRUCTURE OF TELOMERIC DNA OLIGONUCLEOTIDESR01GM048123 · NIGMS · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI FEIGON, JULI · 1992 to 2018
$6.4M
NCRR NIH HHS P41 RR015301NIGMS NIH HHS GM048123NIGMS NIH HHS P41 GM103403NIGMS NIH HHS R01 GM048123
6 · The paper itself

Abstract

Shq1 is an essential protein involved in the early steps of biogenesis and assembly of H/ACA ribonucleoprotein particles (RNPs). Shq1 binds to dyskerin (Cbf5 in yeast) at an early step of H/ACA RNP assembly and is subsequently displaced by the H/ACA RNA. Shq1 contains an N-terminal CS and a C-terminal Shq1-specific domain (SSD). Dyskerin harbors many mutations associated with dyskeratosis congenita. Structures of yeast Shq1 SSD bound to Cbf5 revealed that only a subset of these mutations is in the SSD binding site, implicating another subset in the putative CS binding site. Here, we present the crystal structure of human Shq1 CS (hCS) and the nuclear magnetic resonance (NMR) and crystal structures of hCS containing a serine substitution for proline 22 that is associated with some prostate cancers. The structure of hCS is similar to yeast Shq1 CS domain (yCS) and consists of two β-sheets that form an immunoglobulin-like β-sandwich fold. The N-terminal affinity tag sequence AHHHHHH associates with a neighboring protein in the crystal lattice to form an extra β-strand. Deletion of this tag was required to get spectra suitable for NMR structure determination, while the tag was required for crystallization. NMR chemical shift perturbation (CSP) experiments with peptides derived from putative CS binding sites on dyskerin and Cbf5 revealed a conserved surface on CS important for Cbf5/dyskerin binding. A HADDOCK (high-ambiguity-driven protein-protein docking) model of a Shq1-Cbf5 complex that defines the position of CS domain in the pre-H/ACA RNP was calculated using the CSP data.

Indexed as

Amino Acid SubstitutionBinding SitesCarrier ProteinsCell Cycle ProteinsCrystallography, X-RayDyskeratosis CongenitaHumansHydro-LyasesIntracellular Signaling Peptides and ProteinsMaleMicrotubule-Associated ProteinsMutationNuclear Magnetic Resonance, BiomolecularNuclear ProteinsProstatic NeoplasmsProtein BindingCarrier ProteinsCBF5 protein, S cerevisiaeCell Cycle ProteinsDKC1 protein, humanHydro-LyasesIntracellular Signaling Peptides and ProteinsMicrotubule-Associated ProteinsNuclear ProteinsRibonucleoproteins, Small NuclearRibonucleoproteins, Small NucleolarSaccharomyces cerevisiae ProteinsSHQ1 protein, humanchemical shift perturbationdyskerin and Cbf5NMRtelomeraseX-ray crystal structure

Identifiers

PMID25553844
PMCPMC4323627
OpenAlexW2076725055

What OpenQuestion holds

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Read underepoch 390

Registered trials

None linked

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.