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mfd [2020-09-09 14:40:20]
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mfd [2020-09-09 14:40:20]

transcription-repair coupling factor, eliminates genetic damage from transcriptionally active genes during sporulation, required for increased mutagenesis of lagging strand genes
Locus
BSU_00550
Isoelectric point
5.37
Molecular weight
133.59 kDa
Protein length
1177 aa Sequence Blast
Gene length
3534 bp Sequence Blast
Function
promotes strand-specific DNA repair by displacing
Product
transcription-repair coupling factor
Essential
no
E.C.
3.6.4.-
Synonyms

Genomic Context

      
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Categories containing this gene/protein

Gene

Coordinates
60,430 63,963

Phenotypes of a mutant

  • in an mfd knock-out, the cell's ability to accumulate adaptive mutations in stationary phase is depressed PubMed
  • strongly reduced stationary phase mutagenesis PubMed
  • increased UV-induced mutagenesis via PolY1/ PolY2-mediated translesion synthesis PubMed
  • the mutation suppresses the mucoid phenotype of motA or motB mutants PubMed
  • sensitive to blue light-induced DNA damage PubMed
  • sensitive to oxidative stress PubMed
  • suppression of lethality of pcrA inactvation PubMed
  • The protein

    Catalyzed reaction/ biological activity

  • promotes strand-specific DNA repair by displacing RNA polymerase stalled at a nucleotide lesion and directing the (A)BC excinuclease to RNA damage site
  • is required for roadblock transcription repression by transcription factors with binding sites downstream of the promoter (as for CcpA PubMed and CodY PubMed)
  • required for the processing of genetic damage during sporulation PubMed
  • required for repair of DNA lesions during growth PubMed
  • promotes error-prone DNA repair during stress to promote genetic diversity PubMed
  • Protein family

  • N-terminal part: UvrB family (with UvrB, according to UniProt)
  • C-terminal part: helicase family (according to UniProt)
  • Paralogous protein(s)

    Domains

  • Helicase ATP-binding domain (aa 638-799) (according to UniProt)
  • Helicase C-terminal domain (aa 820-974) (according to UniProt)
  • Structure

  • 2EYQ (Mfd from E. coli) PubMed
  • 3MLQ (RNA polymerase interacting domain of Thermus thermophilus Mfd with the Thermus aquaticus RpoB beta1 domain) PubMed
  • Localization

  • cytoplasm (according to UniProt)
  • Additional information

  • Mfd may interact with RNA polymerase PubMed
  • Expression and Regulation

    Operons

    Biological materials

    Mutant

  • GP1167 (del ermC), available in Jörg Stülke's lab PubMed
  • BKE00550 (mfd::erm, available in the BGSC, in Fabian Commichau's, and in Jörg Stülke's labs) PubMed
  • BKE00550 (mfd::erm trpC2) available at BGSC, PubMed, upstream reverse: _UP1_CATATGGCCCCTCCTCTCTG, downstream forward: _UP4_TAAATTTTGTTACTCTCTGG
  • BKK00550 (mfd::kan trpC2) available at BGSC, PubMed, upstream reverse: _UP1_CATATGGCCCCTCCTCTCTG, downstream forward: _UP4_TAAATTTTGTTACTCTCTGG
  • GFP fusion

  • GP1510 (spc, based on pGP1870, pGP1389-derivative ), available in Jörg Stülke's lab
  • Two-hybrid system

  • B. pertussis adenylate cyclase-based bacterial two hybrid system (BACTH), available in Fabian Commichau's lab
  • Antibody

  • **
  • References

    Reviews

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    Original publications

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