Evidence map›Paper›PMID 19183285›Full record

ArticleMolecular microbiology2009

Controlled degradation by ClpXP protease tunes the levels of the excision repair protein UvrA to the extent of DNA damage.

Mihaela Pruteanu, Tania A Baker

Open access · bronzeAbstract read
In one paragraph

Article in Molecular microbiology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
–field-weighted citation impact, top 95% 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

22 citing papers in PubMed, 1 citations in OpenAlex.

  1. Article
  2. Degron-controlled protein degradation inbioRxiv : the preprint server for biology · 2023
    Article
  3. Proteomic survey of the DNA damage response inJournal of bacteriology · 2023
    Article
  4. Proteomic survey of the DNA damage response inbioRxiv : the preprint server for biology · 2023
    Article
  5. Review
  6. Article
  7. Genome Plasticity ofInfection and immunity · 2018
    Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Review
  15. Review
  16. Review
  17. Article
  18. Article
  19. Circadian control of XPA and excision repair of cisplatin-DNA damage by cryptochrome and HERC2 ubiquitin ligase.Proceedings of the National Academy of Sciences of the United States of America · 2010
    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

2 authors at 2 institutions in 1 country.

Mihaela PruteanuHoward Hughes Medical Institute, Massachusetts Institute of Technology, Cambridge, MA 02139, USA.
Tania A Baker
Howard Hughes Medical Institute · USMassachusetts Institute of Technology · US

Funding

Protein Recognition for Remodeling and Degradation by Bacterial AAA+ ATPasesR01GM049224 · NIGMS · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI BAKER, TANIA A · 1993 to 2013
$4.0M
Howard Hughes Medical InstituteNIGMS NIH HHS GM49224NIGMS NIH HHS R01 GM049224
6 · The paper itself

Abstract

UV irradiation damages DNA and activates expression of genes encoding proteins helpful for survival under DNA stress. These proteins are often deleterious in the absence of DNA damage. Here, we investigate mechanisms used to regulate the levels of DNA-repair proteins during recovery by studying control of the nucleotide excision repair (NER) protein UvrA. We show that UvrA is induced after UV irradiation and reaches maximum levels between approximately 20 and 120 min post UV. During post-UV recovery, UvrA levels decrease principally as a result of ClpXP-dependent protein degradation. The rate of UvrA degradation depends on the amount of unrepaired pyrimidine dimers present; this degradation rate is initially slow shortly after UV, but increases as damage is repaired. This increase in UvrA degradation as repair progresses is also influenced by protein-protein interactions. Genetic and in vitro experiments support the conclusion that UvrA-UvrB interactions antagonize degradation. In contrast, Mfd appears to act as an enhancer of UvrA turnover. Thus, our results reveal that a complex network of interactions contribute to tuning the level of UvrA in the cell in response to the extent of DNA damage and nicely mirror findings with excision repair proteins from eukaryotes, which are controlled by proteolysis in a similar manner.

Indexed as

DNA DamageDNA RepairAdenosine TriphosphatasesBacterial ProteinsDNA, BacterialDNA-Binding ProteinsEndopeptidase ClpEscherichia coliEscherichia coli ProteinsSequence DeletionTranscription FactorsUltraviolet RaysAdenosine TriphosphatasesBacterial ProteinsClpXP protease, E coliDNA, BacterialDNA-Binding ProteinsEndopeptidase ClpEscherichia coli ProteinsTranscription Factorstranscription repair coupling factor protein, BacteriaUvrA protein, E coli

Identifiers

PMID19183285
PMCPMC2867671
OpenAlexW1495004151

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.