Difference between revisions of "Mfd"
(→Original Articles) |
|||
| Line 17: | Line 17: | ||
the (A)BC excinuclease to the RNA damage site | the (A)BC excinuclease to the RNA damage site | ||
|- | |- | ||
| − | |colspan="2" style="background:#FAF8CC;" align="center"| '''Gene expression levels in [http:// | + | |colspan="2" style="background:#FAF8CC;" align="center"| '''Gene expression levels in [http://subtiwiki.uni-goettingen.de/apps/expression/ ''Subti''Express]''': [http://subtiwiki.uni-goettingen.de/apps/expression/expression.php?search=BSU00550 mfd] |
[[RNA polymerase]] stalled at a nucleotide lesion and directing | [[RNA polymerase]] stalled at a nucleotide lesion and directing | ||
| Line 30: | Line 30: | ||
|style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[fin]]'', ''[[spoVT]]'' | |style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[fin]]'', ''[[spoVT]]'' | ||
|- | |- | ||
| − | | | + | |style="background:#FAF8CC;" align="center"|'''Sequences'''||[http://bsubcyc.org/BSUB/sequence-aa?type=GENE&object=BSU00550 Protein] [http://bsubcyc.org/BSUB/sequence?type=GENE&object=BSU00550 DNA] [http://bsubcyc.org/BSUB/seq-selector?chromosome=CHROM-1&object=BSU00550 Advanced_DNA] |
|- | |- | ||
|colspan="2" | '''Genetic context''' <br/> [[Image:mfd_context.gif]] | |colspan="2" | '''Genetic context''' <br/> [[Image:mfd_context.gif]] | ||
Revision as of 11:55, 13 May 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 Advanced_DNA |
Genetic context 
This image was kindly provided by SubtiList
| |
Expression at a glance PubMed
| |
Contents
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:
- UniProt: P37474
- KEGG entry: [2]
- E.C. number:
Additional information
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:
- two-hybrid system:
- Antibody:
Labs working on this gene/protein
Your additional remarks
References
Reviews
Original Articles
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)
