Difference between revisions of "MutS"

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* '''Kinetic information:'''
 
* '''Kinetic information:'''
  
* '''Domains:'''  
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* '''[[Domains]]:'''  
  
 
* '''Modification:'''
 
* '''Modification:'''
  
* '''Cofactor(s):'''
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* '''[[Cofactors]]:'''
  
 
* '''Effectors of protein activity:'''
 
* '''Effectors of protein activity:'''
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* '''Structure:'''
 
* '''Structure:'''
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** [http://www.pdb.org/pdb/explore/explore.do?structureId=1ng9 1NG9] (from ''E. coli'', 39% identity) {{PubMed|12554674}}
  
 
* '''UniProt:''' [http://www.uniprot.org/uniprot/P49849 P49849]
 
* '''UniProt:''' [http://www.uniprot.org/uniprot/P49849 P49849]
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<pubmed> 22933559 </pubmed>
 
<pubmed> 22933559 </pubmed>
 
== Original publications ==
 
== Original publications ==
<pubmed>8760914, 15375129,16479537 20525796 20453097 23228104 21958350 23882084 23998896 24062730 </pubmed>
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<pubmed>8760914, 15375129,16479537 20525796 20453097 23228104 21958350 23882084 23998896 24062730 12554674 </pubmed>
  
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 16:24, 27 February 2014

  • Description: DNA mismatch repair (mismatch recognition protein)

Gene name mutS
Synonyms
Essential no
Product mismatch recognition protein
Function DNA repair
Gene expression levels in SubtiExpress: mutS
Interactions involving this protein in SubtInteract: MutS
MW, pI 97 kDa, 5.189
Gene length, protein length 2574 bp, 858 aa
Immediate neighbours cotE, mutL
Sequences Protein DNA DNA_with_flanks
Genetic context
MutS context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
MutS expression.png















Categories containing this gene/protein

DNA repair/ recombination

This gene is a member of the following regulons

The gene

Basic information

  • Locus tag: BSU17040

Phenotypes of a mutant

Database entries

  • DBTBS entry: [1]
  • SubtiList entry: [2]

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity:
    • MutS recognizes mismatches in the DNA and recruits MutL to the site of mismatch recognition
  • Protein family: DNA mismatch repair mutS family (according to Swiss-Prot)
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Modification:
  • Effectors of protein activity:
  • Localization:
    • forms foci at midcell position, the frequency of foci increases upon mismatch formation PubMed
    • replication-active region of the DNA, via DnaN PubMed

Database entries

  • Structure:
  • KEGG entry: [3]
  • E.C. number:

Additional information

Expression and regulation

  • Regulation:
  • Regulatory mechanism:

Biological materials

  • Expression vector:
  • lacZ fusion:
  • GFP fusion:
  • two-hybrid system:
  • Antibody:

Labs working on this gene/protein

Your additional remarks

References

Reviews

Original publications

Motohiro Akashi, Hirofumi Yoshikawa
Relevance of GC content to the conservation of DNA polymerase III/mismatch repair system in Gram-positive bacteria.
Front Microbiol: 2013, 4;266
[PubMed:24062730] [WorldCat.org] [DOI] (P e)

Justin S Lenhart, Monica C Pillon, Alba Guarné, Lyle A Simmons
Trapping and visualizing intermediate steps in the mismatch repair pathway in vivo.
Mol Microbiol: 2013, 90(4);680-98
[PubMed:23998896] [WorldCat.org] [DOI] (I p)

Nina Y Yao, Jeremy W Schroeder, Olga Yurieva, Lyle A Simmons, Mike E O'Donnell
Cost of rNTP/dNTP pool imbalance at the replication fork.
Proc Natl Acad Sci U S A: 2013, 110(32);12942-7
[PubMed:23882084] [WorldCat.org] [DOI] (I p)

Justin S Lenhart, Anushi Sharma, Manju M Hingorani, Lyle A Simmons
DnaN clamp zones provide a platform for spatiotemporal coupling of mismatch detection to DNA replication.
Mol Microbiol: 2013, 87(3);553-68
[PubMed:23228104] [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)

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)

Nicole M Dupes, Brian W Walsh, Andrew D Klocko, Justin S Lenhart, Heather L Peterson, David A Gessert, Cassie E Pavlick, Lyle A Simmons
Mutations in the Bacillus subtilis beta clamp that separate its roles in DNA replication from mismatch repair.
J Bacteriol: 2010, 192(13);3452-63
[PubMed:20453097] [WorldCat.org] [DOI] (I p)

Jean-Christophe Meile, Ling Juan Wu, S Dusko Ehrlich, Jeff Errington, Philippe Noirot
Systematic localisation of proteins fused to the green fluorescent protein in Bacillus subtilis: identification of new proteins at the DNA replication factory.
Proteomics: 2006, 6(7);2135-46
[PubMed:16479537] [WorldCat.org] [DOI] (P 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)

Meindert H Lamers, Herrie H K Winterwerp, Titia K Sixma
The alternating ATPase domains of MutS control DNA mismatch repair.
EMBO J: 2003, 22(3);746-56
[PubMed:12554674] [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)