Difference between revisions of "Mfd"

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* '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=mfd_60430_63963_1 mfd] {{PubMed|22383849}}
 
* '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=mfd_60430_63963_1 mfd] {{PubMed|22383849}}
  
* '''Sigma factor:'''  
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* '''[[Sigma factor]]:'''  
  
 
* '''Regulation:'''  
 
* '''Regulation:'''  
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=References=
 
=References=
 
==Reviews==
 
==Reviews==
<pubmed>17239578 15063847 17917874 8811173 7968917 15720542 16464004 19023283 22201950 22749141</pubmed>
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<pubmed>17239578 15063847 17917874 8811173 7968917 15720542 16464004 19023283 22201950 22749141 22933559 </pubmed>
 
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== Original publications ==
==Original Articles==
 
 
'''Additional publications:''' {{PubMed|21710567,20702425}}
 
'''Additional publications:''' {{PubMed|21710567,20702425}}
 
<pubmed>8594198,20435731 ,104170,16950921,9535092, 16469698 21699902 22178973 22248542 22960746 </pubmed>
 
<pubmed>8594198,20435731 ,104170,16950921,9535092, 16469698 21699902 22178973 22248542 22960746 </pubmed>
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 17:08, 13 September 2013

  • 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

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

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

Additional publications: PubMed

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)

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)