Evidence map›Paper›PMID 27864884›Full record

ReviewPhotochemistry and photobiology2017

Mfd Protein and Transcription-Repair Coupling in Escherichia coli.

Christopher P Selby

Open access · bronzeAbstract readReview
In one paragraph

Review in Photochemistry and photobiology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
3.3field-weighted citation impact, top 8% 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

36 citing papers in PubMed, 58 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Review
  9. Article
  10. A Peek Inside the Machines of Bacterial Nucleotide Excision Repair.International journal of molecular sciences · 2021
    Review
  11. Mfd regulates RNA polymerase association with hard-to-transcribe regions in vivo, especially those with structured RNAs.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  12. The Role of Pseudo-Orthocaspase (SyOC) ofFrontiers in microbiology · 2021
    Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Review
  20. Formation and Recognition of UV-Induced DNA Damage within Genome Complexity.International journal of molecular sciences · 2020
    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

1 author at 1 institution in 1 country.

Christopher P SelbyDepartment of Biochemistry and Biophysics, University of North Carolina School of Medicine, Chapel Hill, NC.
University of North Carolina at Chapel Hill · US

Funding

Molecular Mechanism of Mammalian DNA Excision Repair, DNA Damage Checkpoints and the Circadian ClockR35GM118102 · NIGMS · UNIV OF NORTH CAROLINA CHAPEL HILL · PI AZIZ SANCAR · 2016 to 2026
$10.6M
Single Nucleotide Resolution Map of Formation and Repair of Bulky Adducts in the Human GenomeR01ES027255 · NIEHS · UNIV OF NORTH CAROLINA CHAPEL HILL · PI SANCAR, AZIZ · 2016 to 2020
$2.3M
NIEHS NIH HHS R01 ES027255NIGMS NIH HHS R35 GM118102
6 · The paper itself

Abstract

In 1989, transcription-repair coupling (TRC) was first described in Escherichia coli, as the transcription-dependent, preferential nucleotide excision repair (NER) of UV photoproducts located in the template DNA strand. This finding led to pioneering biochemical studies of TRC in the laboratory of Professor Aziz Sancar, where, at the time, major contributions were being made toward understanding the roles of the UvrA, UvrB and UvrC proteins in NER. When the repair studies were extended to TRC, template but not coding strand lesions were found to block RNA polymerase (RNAP) in vitro, and unexpectedly, the blocked RNAP inhibited NER. A transcription-repair coupling factor, also called Mfd protein, was found to remove the blocked RNAP, deliver the repair enzyme to the lesion and thereby mediate more rapid repair of the transcription-blocking lesion compared with lesions elsewhere. Structural and functional analyses of Mfd protein revealed helicase motifs responsible for ATP hydrolysis and DNA binding, and regions that interact with RNAP and UvrA. These and additional studies provided a basis upon which other investigators, in following decades, have characterized fascinating and unexpected structural and mechanistic features of Mfd, revealed the possible existence of additional pathways of TRC and discovered additional roles of Mfd in the cell.

Indexed as

DNA RepairTranscription, GeneticAdenosine TriphosphateBacterial ProteinsDNA DamageDNA-Directed RNA PolymerasesEscherichia coliEscherichia coli ProteinsHydrolysisModels, BiologicalProtein ConformationTemplates, GeneticTranscription FactorsUltraviolet RaysAdenosine TriphosphateBacterial ProteinsDNA-Directed RNA PolymerasesEscherichia coli ProteinsTranscription Factorstranscription repair coupling factor protein, Bacteria

Identifiers

PMID27864884
PMCPMC5315624
OpenAlexW2549157240

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.