mutS:Gene: Difference between revisions

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{{GBrowseLink|ecoli_W3110|AC_000091|2854749|2859310|GBrowse(W3110)}}  
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{{GBrowseLink|ecoli_DH10B|NC_010473|2942535|2955340|GBrowse(DH10B)}}
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Revision as of 20:12, 17 August 2011

{{#css:Suppresslinks.css}}<css>h1 .editsection { display:none;} h2 .editsection { display:none;}</css>

Quickview   Gene   Gene Product(s)   Expression   Evolution   On One Page    
Nomenclature Location(s) and DNA Sequence Sequence Features Alleles and Phenotypes Genetic Interactions Genetic Resources Accessions Links References Suggestions

Nomenclature

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See Help:Gene_nomenclature for help with entering information in the Gene Nomenclature table.

Standard name

mutS

Mnemonic

Mutator

Synonyms

ECK2728, b2733, JW2703, fdv, ant, plm[1]

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Notes

Location(s) and DNA Sequence

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See Help:Gene_location for help entering information in the Gene Location and DNA sequence table.

Strain Map location Genome coordinates Genome browsers Sequence links

MG1655

61.54 minutes 

MG1655: 2855115..2857676
<gbrowseImage> name=NC_000913:2855115..2857676 source=MG1655 preset=GeneLocation </gbrowseImage>

REL606

NC_012967: 2751953..2754514
<gbrowseImage> name=NC_012967:2751953..2754514 source=REL606 preset=GeneLocation </gbrowseImage>

BW2952

NC_012759: 2740927..2743488
<gbrowseImage> name=NC_012759:2740927..2743488 source=BW2952 preset=GeneLocation </gbrowseImage>

W3110

 

W3110: 2855749..2858310
<gbrowseImage> name=AC_000091:2855749..2858310 source=W3110 preset=GeneLocation </gbrowseImage>

DH10B

DH10B: 2947657..2950218
<gbrowseImage> name=NC_010473:2947657..2950218 source=DH10B preset=GeneLocation </gbrowseImage>

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Notes

Sequence Features

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See Help:Gene_sequence_features for help in entering sequence features in EcoliWiki.

Feature Type Strain Genomic Location Evidence Reference Notes
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Notes

Alleles and Phenotypes

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See Help:Gene_alleles for how to enter or edit alleles and phenotypes in EcoliWiki.

Allele Nt change(s) AA change(s) Phenotype: Type Phenotype: Description Reference Availability Comments

ΔmutS (Keio:JW2703)

deletion

deletion

PMID:16738554[2]

Shigen
CGSC10126[3]

mutS::Tn5KAN-I-SceI (FB20917)

Insertion at nt 2340 in Minus orientation

PMID:15262929[4]

E. coli Genome Project:FB20917

contains pKD46

mutS::Tn5KAN-I-SceI (FB20918)

Insertion at nt 2340 in Minus orientation

PMID:15262929[4]

E. coli Genome Project:FB20918

does not contain pKD46

mutS201::Tn5

CGSC:7794

mutS215::Tn10

CGSC:7797

mutS3

CGSC:11134

mutS210

CGSC:85420

mutS104::mini-Tn10

CGSC:85448

ΔmutS738::kan

PMID:16738554[2]

CGSC:101976

MutS F596A

F596A

  • Mildly defective ATPase activity
  • Defective MutH activation in vitro
  • Moderately elevated mutation and DNA recombination rates in vivo

PMID:12606120[5]

MutS H760A

H760A

  • Mildly defective ATPase activity
  • Defective MutH activation in vitro
  • Moderately elevated mutation and DNA recombination rates in vivo

PMID:12606120[5]

MutS H728A

H728A

  • Mildly defective ATPase activity
  • Defective MutH activation in vitro
  • Moderately elevated mutation and DNA recombination rates in vivo

PMID:12606120[5]

MutS S668A/T669A

S668A/T669A

  • Modest reduction of Kcat (~three-fold)
  • Fails to activate MMR

PMID:12606120[5]

MutS D693N

D693N

  • Modest reduction of Kcat (~three-fold)
  • Fails to activate MMR

PMID:12606120[5]

MutS S668A/T669A/E694A

S668A/T669A/E694A

  • Defective in DNA binding
  • Defective in MMR
  • Catalyzes ATP hydrolysis better than single E694A mutant

PMID:12606120[5]

MutS K620M

K620M

  • Severely reduced ATP binding capacity
  • Fails to activate MutH in MMR initiation assays

PMID:12606120[5]

MutS E694Q

E694Q

  • Binds ATP better than the wt MutS,but hydrolyzes ATP poorly
  • Supports low-level MutH activation in a mismatch-independent manner

PMID:12606120[5]

MutS F36A

F36A

  • Fails to recognize a mismatch site hence failing to initiate MMR
  • Loses mismatch binding capacity

PMID:12606120[5]

MutS D693A

D693A

  • Binds ATP better than the wt MutS,but hydrolyzes ATP poorly
  • Supports low-level MutH activation in a mismatch-independent manner

PMID:12606120[5]

MutS E38Q

E38Q

  • Binds DNA better than wt MutS
  • Activates MutH ~50% more than the wt MutS in correlation with increased affinity for heteroduplex DNA
  • Completely inactive in MMR and in preventing homologous recombination in vivo

PMID:12606120[5]

MutS E694A

E694A

  • Binds ATP better than the wt MutS,but hydrolyzes ATP poorly
  • Supports low-level MutH activation in a mismatch-independent manner

PMID:12606120[5]

MutS E38A

E38A

  • Exhibits moderately increased affinity for homoduplex DNA in vitro
  • MMR defective in vivo

PMID:12606120[5]

MutS E177A

E177A

  • Unable to form H bonds that link domains I and II
  • Indistinguishable from ΔmutS in the in vivo MMR and recombination assays
  • Possesses a lower affinity for heteroduplex DNA in vitro in the presence of ATP
  • Possesses a higher affinity for homoduplex DNA in vitro in the presence of ATP
  • Hyperactive in activating MutH with 2-fold and 4-fold increases observed relative to the wt MutS for heteroduplex and homoduplex DNA, respectively
  • Reduced ATP hydrolysis

PMID:12606120[5]

MutS T115A

T115A

  • Unable to form H bonds that link domains I and II
  • Indistinguishable from ΔmutS in the in vivo MMR and recombination assays
  • Possesses a lower affinity for heteroduplex DNA in vitro in the presence of ATP
  • Possesses a higher affinity for homoduplex DNA in vitro in the presence of ATP
  • Hyperactive in activating MutH with 2-fold and 4-fold increases observed relative to the wt MutS for heteroduplex and homoduplex DNA, respectively
  • Reduced ATP hydrolysis

PMID:12606120[5]

MutS R197E/R198E

R197E/R198E

  • Disrupts the domain interface more extensively than the E177A or T115A mutation
  • In vivo defects similar to E177A and T115A mutations
  • Relatively normal DNA binding
  • Slightly elevated affinity for homoduplex DNA in the presence of ATP
  • Completely fails to activate MutH in vitro

PMID:12606120[5]

MutS R197E/R198E/R199E

R197E/R198E/R199E

  • Disrupts the domain interface more extensively than the E177A or T115A mutation
  • In vivo defects similar to E177A and T115A mutations
  • Probably results in an unstable protein, which is found in inclusion bodies when over-expressed

PMID:12606120[5]


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Notes

Genetic Interactions

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Interactor Interaction Allele Score(s) Reference(s) Accessions Notes
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Notes

Genetic Resources

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See Help:Gene_resources for help entering information into the Genetic Resources table.

Resource Resource Type Source Notes/Reference

JW2703

Plasmid clone

Shigen

PMID:16769691[6]

Status:Clone OK

Primer 1:GCCAGTGCAATAGAAAATTTCGA

Primer 2:CCaACCAGGCTCTTCAAGCGATA

srlD3131::Tn10

Linked marker

CAG18642 = CGSC7423[3]

est. P1 cotransduction: 32% [7]
Synonyms:zfh-3131::Tn10, zfi-3131::Tn10

cysI95::Tn10

Linked marker

CAG12173 = CGSC7425[3]

est. P1 cotransduction: 30% [7]
Synonyms:cysC95::Tn10

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Notes

Accessions in Other Databases

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See Help:Gene_accessions for help with entering information into the Gene Accessions table.

Database Accession Notes

EcoCyc (EcoliWiki Page)

EcoCyc:EG10625

EchoBASE (EcoliWiki Page)

EchoBASE:EB0620

EcoliGenExpDB (EcoliWiki Page)

EcoliGenExpDB:b2733

ECOL199310CYC (EcoliWiki Page)

ECOL199310CYC:C3294

EcoGene (EcoliWiki Page)

EcoGene:EG10625

ECOO157CYC (EcoliWiki Page)

ECOO157CYC:MUTS

CGSC (EcoliWiki Page)

CGSC:469

ASAP (EcoliWikiPage)

ASAP:ABE-0008977


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Notes

Links

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References

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See Help:References for how to manage references in EcoliWiki.

  1. ↑ Riley, M. et al. (2006) Nucleic Acids Res 34:1-6 (corrected supplemental data from B. Wanner)
  2. ↑ 2.0 2.1 Baba, T et al. (2006) Construction of Escherichia coli K-12 in-frame, single-gene knockout mutants: the Keio collection. Mol. Syst. Biol. 2 2006.0008 PubMed
  3. ↑ 3.0 3.1 3.2 CGSC: The Coli Genetics Stock Center
  4. ↑ 4.0 4.1 Kang, Y et al. (2004) Systematic mutagenesis of the Escherichia coli genome. J. Bacteriol. 186 4921-30 PubMed
  5. ↑ 5.00 5.01 5.02 5.03 5.04 5.05 5.06 5.07 5.08 5.09 5.10 5.11 5.12 5.13 5.14 5.15 5.16 Junop, MS et al. (2003) In vitro and in vivo studies of MutS, MutL and MutH mutants: correlation of mismatch repair and DNA recombination. DNA Repair (Amst.) 2 387-405 PubMed
  6. ↑ Kitagawa, M et al. (2005) Complete set of ORF clones of Escherichia coli ASKA library (a complete set of E. coli K-12 ORF archive): unique resources for biological research. DNA Res. 12 291-9 PubMed
  7. ↑ 7.0 7.1 The Tn10 insertion sites determined by Nichols et al. 1998 (PMID:9829956) were reannotated by alignment with E. coli K-12 genome sequence (GenBank accession NC_000913). P1 contransduction frequencies were calculated using the formula of Wu (PMID:5338813).

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