Mfd

From SubtiWiki
Revision as of 14:57, 11 November 2013 by 134.76.70.252 (talk)
Jump to: navigation, search
  • Description: transcription-repair coupling factor, eliminates genetic damage from transcriptionally active genes during sporulation

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

Gene expression levels in SubtiExpress: mfd

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
Sequences Protein DNA DNA_with_flanks
Genetic context
Mfd context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
Mfd expression.png















Categories containing this gene/protein

DNA repair/ recombination, transcription

This gene is a member of the following regulons

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
  • increased UV-induced mutagenesis via PolY1/ PolY2-mediated translesion synthesis PubMed

Database entries

  • DBTBS entry: no entry
  • SubtiList entry: [1]

Additional information

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:

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
  • KEGG entry: [2]
  • E.C. number:

Additional information

Expression and regulation

  • Operon:
  • Regulation:
  • Regulatory mechanism:
  • Additional information:

Biological materials

  • Mutant: GP1167 (del ermC), available in Stülke lab
  • Expression vector:
  • lacZ fusion:
  • two-hybrid system:
  • Antibody:
  • Strep-tag construct: GP890 (spc, based on pGP1389), available in the Stülke lab

Labs working on this gene/protein

Your additional remarks

References

Reviews

Original publications

Fernando H Ramírez-Guadiana, Rocío Del Carmen Barajas-Ornelas, Víctor M Ayala-García, Ronald E Yasbin, Eduardo Robleto, Mario Pedraza-Reyes
Transcriptional coupling of DNA repair in sporulating Bacillus subtilis cells.
Mol Microbiol: 2013, 90(5);1088-99
[PubMed:24118570] [WorldCat.org] [DOI] (I p)

Kévin Howan, Abigail J Smith, Lars F Westblade, Nicolas Joly, Wilfried Grange, Sylvain Zorman, Seth A Darst, Nigel J Savery, Terence R Strick
Initiation of transcription-coupled repair characterized at single-molecule resolution.
Nature: 2012, 490(7420);431-4
[PubMed:22960746] [WorldCat.org] [DOI] (I p)

Holly Anne Martin, Mario Pedraza-Reyes, Ronald E Yasbin, Eduardo A Robleto
Transcriptional de-repression and Mfd are mutagenic in stressed Bacillus subtilis cells.
J Mol Microbiol Biotechnol: 2011, 21(1-2);45-58
[PubMed:22248542] [WorldCat.org] [DOI] (I p)

Katrin Gunka, Stefan Tholen, Jan Gerwig, Christina Herzberg, Jörg Stülke, Fabian M Commichau
A high-frequency mutation in Bacillus subtilis: requirements for the decryptification of the gudB glutamate dehydrogenase gene.
J Bacteriol: 2012, 194(5);1036-44
[PubMed:22178973] [WorldCat.org] [DOI] (I p)

Olivier Delumeau, François Lecointe, Jan Muntel, Alain Guillot, Eric Guédon, Véronique Monnet, Michael Hecker, Dörte Becher, Patrice Polard, Philippe Noirot
The dynamic protein partnership of RNA polymerase in Bacillus subtilis.
Proteomics: 2011, 11(15);2992-3001
[PubMed:21710567] [WorldCat.org] [DOI] (I p)

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)

Lars F Westblade, Elizabeth A Campbell, Chirangini Pukhrambam, Julio C Padovan, Bryce E Nickels, Valerie Lamour, Seth A Darst
Structural basis for the bacterial transcription-repair coupling factor/RNA polymerase interaction.
Nucleic Acids Res: 2010, 38(22);8357-69
[PubMed:20702425] [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)