Evidence map›Paper›PMID 20877309›Full record

ArticleCell research2011

Structural bases of dimerization of yeast telomere protein Cdc13 and its interaction with the catalytic subunit of DNA polymerase α.

Jia Sun, Yuting Yang, Ke Wan, Ninghui Mao, Tai-Yuan Yu, Yi-Chien Lin, Diane C DeZwaan, Brian C Freeman, Jing-Jer Lin, Neal F Lue and 1 more

Abstract read
In one paragraph

Article in Cell research, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 57 papers.

0numbers the graph read from it
0cells of the map it votes in
57citing papers in PubMed
–field-weighted citation impact
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

57 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Telomeres and Cancer.Life (Basel, Switzerland) · 2021
    Review
  9. Regulation of Antigenic Variation byPathogens (Basel, Switzerland) · 2021
    Review
  10. Review
  11. Article
  12. Roles of OB-Fold Proteins in Replication Stress.Frontiers in cell and developmental biology · 2020
    Review
  13. Review
  14. Article
  15. Emerging roles of CST in maintaining genome stability and human disease.Frontiers in bioscience (Landmark edition) · 2018
    Review
  16. Article
  17. Article
  18. Article
  19. Article
  20. 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

11 authors.

Jia SunHoward Hughes Medical Institute, University of Michigan Medical School, 1150 W. Medical Center Drive, Ann Arbor, MI 48109, USA.
Yuting Yang
Ke Wan
Ninghui Mao
Tai-Yuan Yu
Yi-Chien Lin
Diane C DeZwaan
Brian C Freeman
Jing-Jer Lin
Neal F Lue
Ming Lei

Funding

INTERDISCIPLINARY CARDIOVASCULAR RESEARCH FELLOWSHIPT32HL007121 · NHLBI · UNIVERSITY OF IOWA · PI LONDON, BARRY · 1985 to 2020
$15.1M
ANALYSIS OF TELOMERASE REVERSE TRANSCRIPTASER01GM062631 · NIGMS · WEILL MEDICAL COLL OF CORNELL UNIV · PI LUE, NEAL F · 2001 to 2010
$3.0M
Dynamic signaling by intracellular hormone receptorsR01DK074270 · NIDDK · UNIVERSITY OF ILLINOIS AT URBANA-CHAMPAIGN · PI FREEMAN, BRIAN C · 2006 to 2010
$1.5M
Structure of the Telomere Shelterin ComplexR01GM083015 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI LEI, MING · 2008 to 2012
$1.2M
Howard Hughes Medical InstituteNHLBI NIH HHS T32 HL007121NIDDK NIH HHS DK074270NIDDK NIH HHS R01 DK074270NIGMS NIH HHS GM062631NIGMS NIH HHS GM 083015-01NIGMS NIH HHS R01 GM062631NIGMS NIH HHS R01 GM083015
6 · The paper itself

Abstract

Budding yeast Cdc13-Stn1-Ten1 (CST) complex plays an essential role in telomere protection and maintenance, and has been proposed to be a telomere-specific replication protein A (RPA)-like complex. Previous genetic and structural studies revealed a close resemblance between Stn1-Ten1 and RPA32-RPA14. However, the relationship between Cdc13 and RPA70, the largest subunit of RPA, has remained unclear. Here, we report the crystal structure of the N-terminal OB (oligonucleotide/oligosaccharide binding) fold of Cdc13. Although Cdc13 has an RPA70-like domain organization, the structures of Cdc13 OB folds are significantly different from their counterparts in RPA70, suggesting that they have distinct evolutionary origins. Furthermore, our structural and biochemical analyses revealed unexpected dimerization by the N-terminal OB fold and showed that homodimerization is probably a conserved feature of all Cdc13 proteins. We also uncovered the structural basis of the interaction between the Cdc13 N-terminal OB fold and the catalytic subunit of DNA polymerase α (Pol1), and demonstrated a role for Cdc13 dimerization in Pol1 binding. Analysis of the phenotypes of mutants defective in Cdc13 dimerization and Cdc13-Pol1 interaction revealed multiple mechanisms by which dimerization regulates telomere lengths in vivo. Collectively, our findings provide novel insights into the mechanisms and evolution of Cdc13.

Indexed as

Catalytic DomainCrystallography, X-RayDimerizationDNA Polymerase IMutationProtein BindingProtein Structure, TertiaryReplication Protein ASaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsTelomereTelomere-Binding ProteinsCdc13 protein, S cerevisiaeDNA Polymerase IReplication Protein ASaccharomyces cerevisiae ProteinsTelomere-Binding Proteins

Identifiers

PMID20877309
PMCPMC3193437

What OpenQuestion holds

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Registered trials

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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.