Evidence map›Paper›PMID 19019820›Full record

ArticleThe Journal of biological chemistry2009

Structure and functional studies of the CS domain of the essential H/ACA ribonucleoparticle assembly protein SHQ1.

Mahavir Singh, Fernando A Gonzales, Duilio Cascio, Nathanael Heckmann, Guillaume Chanfreau, Juli Feigon

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
1.5field-weighted citation impact, top 18% 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

16 citing papers in PubMed, 28 citations in OpenAlex.

  1. Article
  2. Crystal structures of the naturally fused CS and cytochrome bActa crystallographica. Section D, Structural biology · 2019
    Article
  3. Review
  4. Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. Article
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

6 authors at 1 institution in 1 country.

Mahavir SinghDepartment of Chemistry and Biochemistry, UCLA, Los Angeles, California 90095, USA.
Fernando A Gonzales
Duilio Cascio
Nathanael Heckmann
Guillaume Chanfreau
Juli Feigon
University of California, Los Angeles · US

Funding

Y-FAMILY POLYMERASES AND CO-FACTORS IN TRANSLESION REPLICATIONP41RR015301 · NCRR · CORNELL UNIVERSITY ITHACA · PI EISENBERG, DAVID · 2001 to 2011
$28.2M
STRUCTURE OF TELOMERIC DNA OLIGONUCLEOTIDESR01GM048123 · NIGMS · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI FEIGON, JULI · 1992 to 2018
$6.4M
CONFORMATIONAL VARIABILITY OF RNAR01GM037254 · NIGMS · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI FEIGON, JULI · 1986 to 2010
$4.2M
NCRR NIH HHS P41 RR015301NIGMS NIH HHS GM37254NIGMS NIH HHS GM48123
6 · The paper itself

Abstract

H/ACA ribonucleoprotein particles are essential for ribosomal RNA and telomerase RNA processing and metabolism. Shq1p has been identified as an essential eukaryotic H/ACA small nucleolar (sno) ribonucleoparticle (snoRNP) biogenesis and assembly factor. Shq1p is postulated to be involved in the early biogenesis steps of H/ACA snoRNP complexes, and Shq1p depletion leads to a specific decrease in H/ACA small nucleolar RNA levels and to defects in ribosomal RNA processing. Shq1p contains two predicted domains as follows: an N-terminal CS (named after CHORD-containing proteins and SGT1) or HSP20-like domain, and a C-terminal region of high sequence homology called the Shq1 domain. Here we report the crystal structure and functional studies of the Saccharomyces cerevisiae Shq1p CS domain. The structure consists of a compact anti-parallel beta-sandwich fold that is composed of two beta-sheets containing four and three beta-strands, respectively, and a short alpha-helix. Deletion studies showed that the CS domain is required for the essential functions of Shq1p. Point mutations in residues Phe-6, Gln-10, and Lys-80 destabilize Shq1p in vivo and induce a temperature-sensitive phenotype with depletion of H/ACA small nucleolar RNAs and defects in rRNA processing. Although CS domains are frequently found in co-chaperones of the Hsp90 molecular chaperone, no interaction was detected between the Shq1p CS domain and yeast Hsp90 in vitro. These results show that the CS domain is essential for Shq1p function in H/ACA snoRNP biogenesis in vivo, possibly in an Hsp90-independent manner.

Indexed as

Crystallography, X-RayHSP90 Heat-Shock ProteinsNuclear ProteinsPoint MutationProtein BindingProtein Structure, SecondaryProtein Structure, TertiaryRibonucleoproteins, Small NuclearRNA, FungalRNA Processing, Post-TranscriptionalRNA, RibosomalSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsHSP90 Heat-Shock ProteinsNuclear ProteinsRibonucleoproteins, Small NuclearRNA, FungalRNA, RibosomalSaccharomyces cerevisiae ProteinsShq1 protein, S cerevisiae

Identifiers

PMID19019820
PMCPMC2615527
OpenAlexW2093723313

What OpenQuestion holds

Textmetadata
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.