Evidence map›Paper›PMID 19013467›Full record

ArticleJournal of molecular biology2009

Cleavage of bacteriophage lambda cI repressor involves the RecA C-terminal domain.

Vitold E Galkin, Xiong Yu, Jakub Bielnicki, Dieudonné Ndjonka, Charles E Bell, Edward H Egelman

Open access · greenAbstract read
In one paragraph

Article in Journal of molecular biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
3.3field-weighted citation impact, top 9% 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

27 citing papers in PubMed, 48 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. CRISPRi-mediated repression of threeJournal of bacteriology · 2025
    Article
  5. Review
  6. Article
  7. Article
  8. CI:Mor interactions in the lysogeny switches ofMicrobiome research reports · 2024
    Article
  9. Article
  10. Mutate or die: Atomic structures explain bacterial SOS induction.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  11. Structural basis for regulation of SOS response in bacteria.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  12. Article
  13. Article
  14. A newly identified prophage-encoded gene,Journal of bacteriology · 2021
    Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Review
  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 2 institutions in 1 country.

Vitold E GalkinDepartment of Biochemistry and Molecular Genetics, University of Virginia, Charlottesville, VA 22908-0733, USA.
Xiong Yu
Jakub Bielnicki
Dieudonné Ndjonka
Charles E Bell
Edward H Egelman
University of Virginia · USThe Ohio State University · US

Funding

STRUCTURAL STUDIES OF RECA FILAMENTSR01GM035269 · NIGMS · YALE UNIVERSITY · PI EGELMAN, EDWARD H. · 1986 to 2016
$5.2M
Structural Studies of RecA-DNA ComplexesR01GM067947 · NIGMS · OHIO STATE UNIVERSITY · PI BELL, CHARLES E · 2003 to 2009
$1.4M
NIGMS NIH HHS GM035269NIGMS NIH HHS GM067947NIGMS NIH HHS R01 GM035269NIGMS NIH HHS R01 GM067947
6 · The paper itself

Abstract

The SOS response to DNA damage in Escherichia coli involves at least 43 genes, all under the control of the LexA repressor. Activation of these genes occurs when the LexA repressor cleaves itself, a reaction catalyzed by an active, extended RecA filament formed on DNA. It has been shown that the LexA repressor binds within the deep groove of this nucleoprotein filament, and presumably, cleavage occurs in this groove. Bacteriophages, such as lambda, have repressors (cI) that are structural homologs of LexA and also undergo self-cleavage when SOS is induced. It has been puzzling that some mutations in RecA that affect the cleavage of repressors are in the C-terminal domain (CTD) far from the groove where cleavage is thought to occur. In addition, it has been shown that the rate of cleavage of cI by RecA is dependent upon both the substrate on which RecA is polymerized and the ATP analog used. Electron microscopy and three-dimensional reconstructions show that the conformation and dynamics of RecA's CTD are also modulated by the polynucleotide substrate and ATP analog. Under conditions where the repressor cleavage rates are the highest, cI is coordinated within the groove by contacts with RecA's CTD. These observations provide a framework for understanding previous genetic and biochemical observations.

Indexed as

HydrolysisMicroscopy, Atomic ForceMicroscopy, ElectronProtein ConformationRec A RecombinasesRepressor ProteinsViral Regulatory and Accessory Proteinsphage repressor proteinsRec A RecombinasesRepressor ProteinsViral Regulatory and Accessory Proteins

Identifiers

PMID19013467
PMCPMC2648975
OpenAlexW2064981931

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.