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mfd transcription-repair coupling factor [ Escherichia coli str. K-12 substr. MG1655 ]

Gene ID: 945681, updated on 10-Oct-2024

Summary

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Official Symbol
mfd
Official Full Name
transcription-repair coupling factor
Primary source
ECOCYC:EG11619
Locus tag
b1114
See related
ASAP:ABE-0003763
Gene type
protein coding
RefSeq status
PROVISIONAL
Organism
Escherichia coli str. K-12 substr. MG1655 (strain: K-12, substrain: MG1655)
Lineage
Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia
Also known as
ECK1100
Summary
Mfd dissociates transcription elongation complexes blocked at nonpairing lesions and mediates recruitment of DNA repair proteins. [More information is available at EcoGene: EG11619]. The Mfd (mutation frequency decline) protein, also known as transcription-repair coupling factor , is responsible for ATP-dependent removal of stalled RNA polymerase from DNA lesions by inducing forward movement of the RNA polymerase and subsequent recruitment of nucleotide excision repair machinery to the sites of the lesions . [More information is available at EcoCyc: EG11619].
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Genomic context

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Sequence:
NC_000913.3 (1170518..1173964, complement)

NC_000913.3Genomic Context describing neighboring genes Neighboring gene DUF1471 domain-containing multiple stress resistance outer membrane protein BhsA Neighboring gene ncRNA Neighboring gene L,D-transpeptidase LdtC Neighboring gene inner membrane protein YcfT Neighboring gene lipoprotein release complex - inner membrane subunit Neighboring gene lipoprotein release complex - ATP binding subunit

Genomic regions, transcripts, and products

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Genomic Sequence:
NC_000913.3

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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Related articles in PubMed

  1. Structural basis for transcription complex disruption by the Mfd translocase. Kang JY, et al. Elife, 2021 Jan 22. PMID 33480355, Free PMC Article
  2. Transcription-repair coupling determines the strandedness of ultraviolet mutagenesis in Escherichia coli. Oller AR, et al. Proc Natl Acad Sci U S A, 1992 Nov 15. PMID 1438310, Free PMC Article
  3. Structure and function of transcription-repair coupling factor. II. Catalytic properties. Selby CP, et al. J Biol Chem, 1995 Mar 3. PMID 7876262
  4. Mechanisms of transcription-repair coupling and mutation frequency decline. Selby CP, et al. Microbiol Rev, 1994 Sep. PMID 7968917, Free PMC Article
  5. Molecular mechanism of transcription-repair coupling. Selby CP, et al. Science, 1993 Apr 2. PMID 8465200

See all (47) citations in PubMed

GeneRIFs: Gene References Into Functions

What's a GeneRIF?
  1. Structural basis for transcription complex disruption by the Mfd translocase.
    Title: Structural basis for transcription complex disruption by the Mfd translocase.
  2. Cotranscriptional R-loop formation by Mfd involves topological partitioning of DNA.
    Title: Cotranscriptional R-loop formation by Mfd involves topological partitioning of DNA.
  3. Mfd can locate a stalled/paused transcription elongation complex via a release and catch-up mechanism. Depending on load, Mfd either rescues a backtracked TEC or terminates transcription.
    Title: Mfd Dynamically Regulates Transcription via a Release and Catch-Up Mechanism.
  4. The results reveal that bacterial RNA polymerase is frequently rescued by Mfd during normal growth and highlight a ubiquitous house-keeping role for Mfd in regulating transcription elongation.
    Title: The transcription-repair coupling factor Mfd associates with RNA polymerase in the absence of exogenous damage.
  5. Mfd, which is an ATP-dependent superfamily 2 helicase that binds to RNAP, continues to translocate along DNA after RNAP has been displaced until a lesion in the template strand is located.
    Title: Stalled transcription complexes promote DNA repair at a distance.
  6. TRCF derepression is associated with profound conformational changes that primarily involve a reorganization of the interdomain interactions.
    Title: Derepression of bacterial transcription-repair coupling factor is associated with a profound conformational change.
  7. Mfd might form a excinuclease ABC subunit A recruitment factor at stalled transcription complexes that architecturally
    Title: Structural basis for transcription-coupled repair: the N terminus of Mfd resembles UvrB with degenerate ATPase motifs.
  8. preliminary structure determination of Escherichia coli Mfd, the transcription-repair coupling factor
    Title: Crystallization and preliminary structure determination of Escherichia coli Mfd, the transcription-repair coupling factor.
Submit: New GeneRIF Correction

General gene information

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Homology

Gene Ontology Provided by EcoCyc

Function Evidence Code Pubs
enables ATP binding IEA
Inferred from Electronic Annotation
more info
  
enables DNA binding IBA
Inferred from Biological aspect of Ancestor
more info
  
enables DNA binding IDA
Inferred from Direct Assay
more info
 PubMed 
enables DNA binding IEA
Inferred from Electronic Annotation
more info
  
enables DNA translocase activity IBA
Inferred from Biological aspect of Ancestor
more info
  
enables DNA translocase activity IDA
Inferred from Direct Assay
more info
 PubMed 
enables RNA polymerase core enzyme binding IBA
Inferred from Biological aspect of Ancestor
more info
  
enables RNA polymerase core enzyme binding IDA
Inferred from Direct Assay
more info
 PubMed 
enables damaged DNA binding IEA
Inferred from Electronic Annotation
more info
  
NOT enables helicase activity IDA
Inferred from Direct Assay
more info
 PubMed 
enables hydrolase activity IEA
Inferred from Electronic Annotation
more info
  
enables protein binding IPI
Inferred from Physical Interaction
more info
 PubMed 
Process Evidence Code Pubs
acts_upstream_of_or_within DNA damage response IDA
Inferred from Direct Assay
more info
 PubMed 
involved_in DNA repair IEA
Inferred from Electronic Annotation
more info
  
acts_upstream_of_or_within DNA repair IMP
Inferred from Mutant Phenotype
more info
 PubMed 
involved_in nucleotide-excision repair, preincision complex assembly NAS
Non-traceable Author Statement
more info
 PubMed 
involved_in regulation of DNA-templated transcription IBA
Inferred from Biological aspect of Ancestor
more info
  
acts_upstream_of_or_within regulation of DNA-templated transcription IDA
Inferred from Direct Assay
more info
 PubMed 
involved_in regulation of DNA-templated transcription IEA
Inferred from Electronic Annotation
more info
  
acts_upstream_of_or_within transcription-coupled nucleotide-excision repair EXP
Inferred from Experiment
more info
 PubMed 
acts_upstream_of_or_within transcription-coupled nucleotide-excision repair IDA
Inferred from Direct Assay
more info
 PubMed 
acts_upstream_of_or_within transcription-coupled nucleotide-excision repair IMP
Inferred from Mutant Phenotype
more info
 PubMed 
involved_in transcription-coupled nucleotide-excision repair, DNA damage recognition IBA
Inferred from Biological aspect of Ancestor
more info
  
acts_upstream_of_or_within transcription-coupled nucleotide-excision repair, DNA damage recognition IDA
Inferred from Direct Assay
more info
 PubMed 
involved_in transcription-coupled nucleotide-excision repair, DNA damage recognition IEA
Inferred from Electronic Annotation
more info
  
Component Evidence Code Pubs
part_of DNA repair complex IPI
Inferred from Physical Interaction
more info
 PubMed 
located_in cytoplasm IEA
Inferred from Electronic Annotation
more info
  
located_in cytosol IDA
Inferred from Direct Assay
more info
 PubMed 

General protein information

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Preferred Names
transcription-repair coupling factor

NCBI Reference Sequences (RefSeq)

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Genome Annotation

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference assembly

Genomic

  1. NC_000913.3 Reference assembly

    Range
    1170518..1173964 complement
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. NP_415632.1 transcription-repair coupling factor [Escherichia coli str. K-12 substr. MG1655]

    See identical proteins and their annotated locations for NP_415632.1

    Status: PROVISIONAL

    UniProtKB/TrEMBL
    A0A8S7EJ55, A0A9P2MJT3
    Conserved Domains (1) summary
    PRK10689
    Location:1 → 1147
    PRK10689; transcription-repair coupling factor; Provisional
Nucleotide Protein
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