Evidence map›Paper›PMID 18836076›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2008

Mms19 protein functions in nucleotide excision repair by sustaining an adequate cellular concentration of the TFIIH component Rad3.

Haiping Kou, Ying Zhou, R M Charlotte Gorospe, Zhigang Wang

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
0.6field-weighted citation impact, top 33% 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

14 citing papers in PubMed, 31 citations in OpenAlex.

  1. Review
  2. Review
  3. Biogenesis of Iron-Sulfur Clusters and Their Role in DNA Metabolism.Frontiers in cell and developmental biology · 2021
    Review
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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

4 authors at 1 institution in 1 country.

Haiping KouGraduate Center for Toxicology, University of Kentucky, Lexington, KY 40536, USA.
Ying Zhou
R M Charlotte Gorospe
Zhigang Wang
University of Kentucky · US

Funding

MOLECULAR DISSECTION OF YEAST NUCLEOTIDE EXCISION REPAIRR01CA067978 · NCI · UNIVERSITY OF KENTUCKY · PI WANG, ZHIGANG · 1997 to 2006
$1.3M
MOLECULAR DISSECTION OF YEAST NUCLEOTIDE EXCISION REPAIRR55CA067978 · NCI · UNIVERSITY OF TEXAS SW MED CTR/DALLAS · PI WANG, ZHIGANG · 1995 to 1995
–
NCI NIH HHS CA67978NCI NIH HHS R01 CA067978NCI NIH HHS R55 CA067978
6 · The paper itself

Abstract

Nucleotide excision repair (NER) is a major cellular defense mechanism against DNA damage. We have investigated the role of Mms19 in NER in the yeast Saccharomyces cerevisiae. NER was deficient in the mms19 deletion mutant cell extracts, which was complemented by the NER/transcription factor TFIIH, but not by purified Mms19 protein. In mms19 mutant cells, protein levels of the core TFIIH component Rad3 (XPD homologue) and Ssl2 (XPB homologue) were significantly reduced by up to 3.5- and 2.2-fold, respectively. The other four essential subunits of the core TFIIH, Tfb1, Tfb2, Ssl1, and Tfb4, and the TFIIK subunits Tfb3, Kin28, and Ccl1 of the holo TFIIH were not much affected by Mms19. Elevating Rad3 protein concentration by overexpressing the protein from a plasmid under the GAL1 promoter control restored proficient NER in mms19 mutant cells, as indicated by complementation for UV sensitivity. Overexpression of Ssl2 had no effect on repair. Overexpression of Rad3, Ssl2, or both proteins, however, could not correct the temperature-sensitive growth defect of mms19 mutant cells. These results show that Mms19 functions in NER by sustaining an adequate cellular concentration of the TFIIH component Rad3 and suggest that Mms19 has distinct and separable functions in NER and cell growth, thus implicating Mms19 protein as a novel multifunctional regulator in cells.

Indexed as

DNA RepairTranscription Factor TFIIHDNA HelicasesGene Expression Regulation, FungalSaccharomyces cerevisiae ProteinsTranscription FactorsDNA HelicasesMET18 protein, S cerevisiaeRad3 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsSSL2 protein, S cerevisiaeTranscription FactorsTranscription Factor TFIIH

Identifiers

PMID18836076
PMCPMC2572961
OpenAlexW2035314287

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.