Mfd

• Description: transcription-repair coupling factor
  
  

Gene name	mfd
Synonyms
Essential	no
Product	transcription-repair coupling factor
Function	promotes strand-specific DNA repair by displacing RNA polymerase stalled at a nucleotide lesion and directing the (A)BC excinuclease to the RNA damage site
Interactions involving this protein in SubtInteract: Mfd
MW, pI	133 kDa, 5.367
Gene length, protein length	3531 bp, 1177 aa
Immediate neighbours	fin, spoVT
Get the DNA and protein sequences (Barbe et al., 2009)
Genetic context This image was kindly provided by SubtiList

Categories containing this gene/protein

DNA repair/ recombination, transcription

The gene

Basic information

• Locus tag: BSU00550

Phenotypes of a mutant

In an mfd knock-out, the cell's ability to accumulate adaptive mutations in stationary phase is depressed. PubMed

Database entries

• DBTBS entry: no entry

• SubtiList entry: [1]

The protein

Basic information/ Evolution

• 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 the 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)

• Protein family:

• Paralogous protein(s): RecG

Extended information on the protein

• Kinetic information:

• Domains:

• Modification:

• Cofactor(s):

• Effectors of protein activity:

• Interactions:
  • Mfd interacts with the RNA polymerase PubMed
  • Mfd-UvrA PubMed
  • Mfd-RpoB PubMed

• Localization:

Database entries

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

• UniProt: P37474

• KEGG entry: [2]

• E.C. number:

Expression and regulation

• Operon:

• Sigma factor:

• Regulation:

• Regulatory mechanism:

• Additional information:

Biological materials

• Mutant: GP1167 (del ermC), available in Stülke lab

• Expression vector:

• lacZ fusion:

• GFP fusion: GP1510 (spc, based on pGP1870, pGP1389-derivative ), available in the Stülke lab

• YFP fusion: GP1511 (spc, based on pGP1871, pGP1389-derivative ), available in the Stülke lab

• two-hybrid system:

• Antibody:

• Strep-tag construct: GP890 (spc, based on pGP1389), available in the Stülke lab

References

Original Articles

Additional publications: PubMed

Boris R Belitsky, Abraham L Sonenshein
Roadblock repression of transcription by Bacillus subtilis CodY.
J Mol Biol: 2011, 411(4);729-43
[PubMed:21699902] [WorldCat.org] [DOI] (I p)

Christine Pybus, Mario Pedraza-Reyes, Christian A Ross, Holly Martin, Katherine Ona, Ronald E Yasbin, Eduardo Robleto
Transcription-associated mutation in Bacillus subtilis cells under stress.
J Bacteriol: 2010, 192(13);3321-8
[PubMed:20435731] [WorldCat.org] [DOI] (I p)

Christian Ross, Christine Pybus, Mario Pedraza-Reyes, Huang-Mo Sung, Ronald E Yasbin, Eduardo Robleto
Novel role of mfd: effects on stationary-phase mutagenesis in Bacillus subtilis.
J Bacteriol: 2006, 188(21);7512-20
[PubMed:16950921] [WorldCat.org] [DOI] (P p)

Alexandra M Deaconescu, Anna L Chambers, Abigail J Smith, Bryce E Nickels, Ann Hochschild, Nigel J Savery, Seth A Darst
Structural basis for bacterial transcription-coupled DNA repair.
Cell: 2006, 124(3);507-20
[PubMed:16469698] [WorldCat.org] [DOI] (P p)

J M Zalieckas, L V Wray, A E Ferson, S H Fisher
Transcription-repair coupling factor is involved in carbon catabolite repression of the Bacillus subtilis hut and gnt operons.
Mol Microbiol: 1998, 27(5);1031-8
[PubMed:9535092] [WorldCat.org] [DOI] (P p)

S Ayora, F Rojo, N Ogasawara, S Nakai, J C Alonso
The Mfd protein of Bacillus subtilis 168 is involved in both transcription-coupled DNA repair and DNA recombination.
J Mol Biol: 1996, 256(2);301-18
[PubMed:8594198] [WorldCat.org] [DOI] (P p)

V D Filippov, E E Zagoruiko
Study of MFD in Bacillus subtilis.
Mutat Res: 1978, 52(1);49-56
[PubMed:104170] [WorldCat.org] [DOI] (P p)