Evidence map›Paper›PMID 19700770›Full record

ArticleNucleic acids research2009

An N-terminal clamp restrains the motor domains of the bacterial transcription-repair coupling factor Mfd.

Michael N Murphy, Peng Gong, Kenneth Ralto, Laura Manelyte, Nigel J Savery, Karsten Theis

Abstract read
In one paragraph

Article in Nucleic acids research, 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
–field-weighted citation impact
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.

  1. Article
  2. Article
  3. Review
  4. Review
  5. Article
  6. A Peek Inside the Machines of Bacterial Nucleotide Excision Repair.International journal of molecular sciences · 2021
    Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Uncoupling of ProteaseJournal of virology · 2017
    Article
  12. Review
  13. Article
  14. Article
  15. Regulation of Transcript Elongation.Annual review of microbiology · 2015
    Review
  16. UvrD helicase: an old dog with a new trick: how one step backward leads to many steps forward.BioEssays : news and reviews in molecular, cellular and developmental biology · 2015
    Review
  17. Regulation of the Rhp26ERCC6/CSB chromatin remodeler by a novel conserved leucine latch motif.Proceedings of the National Academy of Sciences of the United States of America · 2014
    Article
  18. RNA polymerase between lesion bypass and DNA repair.Cellular and molecular life sciences : CMLS · 2013
    Review
  19. Prokaryotic nucleotide excision repair.Cold Spring Harbor perspectives in biology · 2013
    Review
  20. Review
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.

Michael N MurphyDepartment of Chemistry, Department of Biochemistry & Molecular Biology, University of Massachusetts Amherst, Amherst, Massachusetts 01003, USA.
Peng Gong
Kenneth Ralto
Laura Manelyte
Nigel J Savery
Karsten Theis

Funding

Biotechnology and Biological Sciences Research Council BB/E004695Biotechnology and Biological Sciences Research Council BB/E004695/1
6 · The paper itself

Abstract

Motor proteins that translocate on nucleic acids are key players in gene expression and maintenance. While the function of these proteins is diverse, they are driven by highly conserved core motor domains. In transcription-coupled DNA repair, motor activity serves to remove RNA polymerase stalled on damaged DNA, making the lesion accessible for repair. Structural and biochemical data on the bacterial transcription-repair coupling factor Mfd suggest that this enzyme undergoes large conformational changes from a dormant state to an active state upon substrate binding. Mfd can be functionally dissected into an N-terminal part instrumental in recruiting DNA repair proteins (domains 1-3, MfdN), and a C-terminal part harboring motor activity (domains 4-7, MfdC). We show that isolated MfdC has elevated ATPase and motor activities compared to the full length protein. While MfdN has large effects on MfdC activity and thermostability in cis, these effects are not observed in trans. The structure of MfdN is independent of interactions with MfdC, implying that MfdN acts as a clamp that restrains motions of the motor domains in the dormant state. We conclude that releasing MfdN:MfdC interactions serves as a central molecular switch that upregulates Mfd functions during transcription-coupled DNA repair.

Indexed as

Adenosine TriphosphatasesBacterial ProteinsDNAModels, MolecularProtein Structure, TertiaryTemperatureTranscription FactorsAdenosine TriphosphatasesBacterial ProteinsDNATranscription Factorstranscription repair coupling factor protein, Bacteria

Identifiers

PMID19700770
PMCPMC2764443

What OpenQuestion holds

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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.