Difference between revisions of "MutL"
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[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] |
Revision as of 13:35, 27 May 2013
- Description: DNA mismatch repair
Gene name | mutL |
Synonyms | |
Essential | no |
Product | DNA mismatch repair |
Function | DNA repair |
Gene expression levels in SubtiExpress: mutL | |
Interactions involving this protein in SubtInteract: MutL | |
MW, pI | 70 kDa, 5.583 |
Gene length, protein length | 1881 bp, 627 aa |
Immediate neighbours | mutS, ymzD |
Sequences | Protein DNA DNA_with_flanks |
Genetic context This image was kindly provided by SubtiList
| |
Expression at a glance PubMed |
Contents
Categories containing this gene/protein
This gene is a member of the following regulons
The gene
Basic information
- Locus tag: BSU17050
Phenotypes of a mutant
Database entries
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity:
- Protein family: DNA mismatch repair mutL/hexB family (according to Swiss-Prot)
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Domains:
- Modification:
- Cofactor(s):
- Effectors of protein activity:
- Localization:
- forms foci at midcell position, the frequency of foci increases upon mismatch formation PubMed
Database entries
- UniProt: P49850
- KEGG entry: [3]
- E.C. number:
Additional information
Expression and regulation
- Sigma factor:
- Regulation:
- Regulatory mechanism:
Biological materials
- Mutant: GP1190 (del mutSL::aphA3) available in the Stülke lab
- Expression vector:
- lacZ fusion:
- GFP fusion:
- two-hybrid system:
- Antibody:
Labs working on this gene/protein
Your additional remarks
References
Nicholas J Bolz, Justin S Lenhart, Steven C Weindorf, Lyle A Simmons
Residues in the N-terminal domain of MutL required for mismatch repair in Bacillus subtilis.
J Bacteriol: 2012, 194(19);5361-7
[PubMed:22843852]
[WorldCat.org]
[DOI]
(I p)
Andrew D Klocko, Jeremy W Schroeder, Brian W Walsh, Justin S Lenhart, Margery L Evans, Lyle A Simmons
Mismatch repair causes the dynamic release of an essential DNA polymerase from the replication fork.
Mol Microbiol: 2011, 82(3);648-63
[PubMed:21958350]
[WorldCat.org]
[DOI]
(I p)
Monica C Pillon, Jeffrey H Miller, Alba Guarné
The endonuclease domain of MutL interacts with the β sliding clamp.
DNA Repair (Amst): 2011, 10(1);87-93
[PubMed:21050827]
[WorldCat.org]
[DOI]
(I p)
Monica C Pillon, Jessica J Lorenowicz, Michael Uckelmann, Andrew D Klocko, Ryan R Mitchell, Yu Seon Chung, Paul Modrich, Graham C Walker, Lyle A Simmons, Peter Friedhoff, Alba Guarné
Structure of the endonuclease domain of MutL: unlicensed to cut.
Mol Cell: 2010, 39(1);145-51
[PubMed:20603082]
[WorldCat.org]
[DOI]
(I p)
Irnov Irnov, Cynthia M Sharma, Jörg Vogel, Wade C Winkler
Identification of regulatory RNAs in Bacillus subtilis.
Nucleic Acids Res: 2010, 38(19);6637-51
[PubMed:20525796]
[WorldCat.org]
[DOI]
(I p)
Mario Pedraza-Reyes, Ronald E Yasbin
Contribution of the mismatch DNA repair system to the generation of stationary-phase-induced mutants of Bacillus subtilis.
J Bacteriol: 2004, 186(19);6485-91
[PubMed:15375129]
[WorldCat.org]
[DOI]
(P p)
F Ginetti, M Perego, A M Albertini, A Galizzi
Bacillus subtilis mutS mutL operon: identification, nucleotide sequence and mutagenesis.
Microbiology (Reading): 1996, 142 ( Pt 8);2021-9
[PubMed:8760914]
[WorldCat.org]
[DOI]
(P p)