Evidence map›Paper›PMID 16227619›Full record

ArticleMolecular and cellular biology2005

Complex formation of yeast Rev1 and Rev7 proteins: a novel role for the polymerase-associated domain.

Narottam Acharya, Lajos Haracska, Robert E Johnson, Ildiko Unk, Satya Prakash, Louise Prakash

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In one paragraph

Article in Molecular and cellular biology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 54 papers.

0numbers the graph read from it
0cells of the map it votes in
54citing papers in PubMed
2.8field-weighted citation impact, top 10% 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

54 citing papers in PubMed, 92 citations in OpenAlex.

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  13. Rev7 dimerization is important for assembly and function of the Rev1/Polζ translesion synthesis complex.Proceedings of the National Academy of Sciences of the United States of America · 2018
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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 2 institutions in 2 countries.

Narottam AcharyaSealy Center for Molecular Science, University of Texas Medical Branch at Galveston, 6.104 Blocker Medical Research Building, 11th and Mechanic Streets, Galveston, TX 77555-1061, USA.
Lajos Haracska
Robert E Johnson
Ildiko Unk
Satya Prakash
Louise Prakash
The University of Texas Medical Branch at Galveston · USInstitute of Genetics · HU

Funding

Translesion synthesis by yeast DNA polymerasesR01CA107650 · NCI · UNIVERSITY OF TEXAS MEDICAL BR GALVESTON · PI PRAKASH, LOUISE · 2004 to 2013
$3.9M
NCI NIH HHS CA 107650NCI NIH HHS R01 CA107650
6 · The paper itself

Abstract

The Rev1 protein of Saccharomyces cerevisiae functions in translesion synthesis (TLS) together with DNA polymerase (Pol) zeta, which is comprised of the Rev3 catalytic and the Rev7 accessory subunits. Rev1, a member of the Y family of Pols, differs from other members in its high degree of specificity for incorporating a C opposite template G as well as opposite an abasic site. Although Rev1 is indispensable for Polzeta-dependent TLS, its DNA synthetic activity is not required for many of the Polzeta-dependent lesion bypass events. This observation has suggested a structural role for Rev1 in this process. Here we show that in yeast, Rev1 forms a stable complex with Rev7, and the two proteins copurify. Importantly, the polymerase-associated domain (PAD) of Rev1 mediates its binding to Rev7. These observations reveal a novel role for the PAD region of Rev1 in protein-protein interactions, and they raise the possibility of a similar involvement of the PAD of other Y family Pols in protein-protein interactions. We discuss the possible roles of Rev1 versus the Rev1-Rev7 complex in TLS.

Indexed as

DNA-Directed DNA PolymeraseNucleotidyltransferasesProtein BindingProtein Structure, TertiarySaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsTwo-Hybrid System TechniquesY-Family DNA PolymerasesDNA-Directed DNA PolymeraseNucleotidyltransferasesREV1 protein, S cerevisiaeREV7 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsY-Family DNA Polymerases

Identifiers

PMID16227619
PMCPMC1265840
OpenAlexW2102091313

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.