Evidence map›Paper›PMID 20159559›Full record

ArticleMolecular cell2010

Unconventional ubiquitin recognition by the ubiquitin-binding motif within the Y family DNA polymerases iota and Rev1.

Martha G Bomar, Sanjay D'Souza, Marzena Bienko, Ivan Dikic, Graham C Walker, Pei Zhou

Open access · bronzeAbstract read
In one paragraph

Article in Molecular cell, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.

0numbers the graph read from it
0cells of the map it votes in
44citing papers in PubMed
4.1field-weighted citation impact, top 5% 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

44 citing papers in PubMed, 74 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Emerging Roles of Non-proteolytic Ubiquitination in Tumorigenesis.Frontiers in cell and developmental biology · 2022
    Review
  6. Review
  7. Protein-Protein Interactions in Translesion Synthesis.Molecules (Basel, Switzerland) · 2021
    Review
  8. Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. Translesion DNA polymerases in eukaryotes: what makes them tick?Critical reviews in biochemistry and molecular biology · 2017
    Review
  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

6 authors at 4 institutions in 2 countries.

Martha G BomarDepartment of Biochemistry, Duke University Medical Center, Durham, NC 27710, USA.
Sanjay D'Souza
Marzena Bienko
Ivan Dikic
Graham C Walker
Pei Zhou
Goethe University Frankfurt · DEMassachusetts Institute of Technology · USDuke Medical Center · USDuke University Hospital · US

Funding

TOXICOLOGY CORE UNITP30ES002109 · NIEHS · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI LEVINE, STUART S · 1985 to 2020
$25.6M
Mechanism of Eukaryotic Environmental MutagenesisR01ES015818 · NIEHS · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI WALKER, GRAHAM C · 2007 to 2016
$3.8M
Structural, Biochemical and Functional Studies of RNAPII CTD Interacting ProteinsR01GM079376 · NIGMS · DUKE UNIVERSITY · PI ZHOU, PEI · 2008 to 2011
$1.2M
Mechanism of Eukaryotic Environmental MutagenesisR56ES015818 · NIEHS · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI WALKER, GRAHAM C · 2011 to 2011
$200k
NIEHS NIH HHS ES-015818NIEHS NIH HHS P30 ES-002109NIEHS NIH HHS P30 ES002109NIEHS NIH HHS R01 ES015818NIEHS NIH HHS R56 ES015818NIGMS NIH HHS GM-079376NIGMS NIH HHS R01 GM079376
6 · The paper itself

Abstract

Translesion synthesis is an essential cell survival strategy to promote replication after DNA damage. The accumulation of Y family polymerases (pol) iota and Rev1 at the stalled replication machinery is mediated by the ubiquitin-binding motifs (UBMs) of the polymerases and enhanced by PCNA monoubiquitination. We report the solution structures of the C-terminal UBM of human pol iota and its complex with ubiquitin. Distinct from other ubiquitin-binding domains, the UBM binds to the hydrophobic surface of ubiquitin centered at L8. Accordingly, mutation of L8A, but not I44A, of ubiquitin abolishes UBM binding. Human pol iota contains two functional UBMs, both contributing to replication foci formation. In contrast, only the second UBM of Saccharomyces cerevisiae Rev1 binds to ubiquitin and is essential for Rev1-dependent cell survival and mutagenesis. Point mutations disrupting the UBM-ubiquitin interaction also impair the accumulation of pol iota in replication foci and Rev1-mediated DNA damage tolerance in vivo.

Indexed as

Amino Acid SequenceDNA DamageDNA-Directed DNA PolymeraseDNA Polymerase iotaHumansMolecular Sequence DataNucleotidyltransferasesProtein Structure, TertiarySaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSequence AlignmentUbiquitinUbiquitinationY-Family DNA PolymerasesDNA-Directed DNA PolymeraseDNA Polymerase iotaNucleotidyltransferasesREV1 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsUbiquitinY-Family DNA Polymerases

Identifiers

PMID20159559
PMCPMC2841503
OpenAlexW2169354964

What OpenQuestion holds

Textmetadata
LicenceTDM
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.