mutS:Gene Product(s)

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Nomenclature Function Interactions Localization Sequence Domains Structure Resources Accessions Links References Suggestions

Nomenclature

See Help:Product_nomenclature for help entering or editing information in this section of EcoliWiki.

Standard name

MutS

Synonyms

methyl-directed mismatch repair protein[1], B2733[2][1], Plm[2][1], Ant[2][1], Fdv[2][1], MutS[2][1] , ant, ECK2728, fdv, JW2703, plm, b2733

Product description

MutS[2][3];

Component of MutHLS complex, methyl-directed mismatch repair[2][3]

Methyl-directed mismatch repair protein; dimeric/tetrameric[4]

EC number (for enzymes)


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Notes

Function

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<protect> Gene Ontology
See Help:Gene_ontology for help entering or editing GO terms and GO annotations in EcoliWiki.

Qualifier GO ID GO term name Reference Evidence Code with/from Aspect Notes Status
GO:0006298

mismatch repair

PMID:6987663[5]

IMP: Inferred from Mutant Phenotype

P

complete

GO:0030983

mismatched DNA binding

PMID:3014530[6]

IDA: Inferred from Direct Assay

F

complete

GO:0006298

mismatch repair

PMID:2665076[7]

IDA: Inferred from Direct Assay

P

complete

GO:0016887

ATPase activity

PMID:10715140[8]

IDA: Inferred from Direct Assay

F

complete

GO:0000166

nucleotide binding

GOA:spkw
SP_KW:GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0547

F

Seeded from EcoCyc (v14.0)

complete

GO:0032300

mismatch repair complex

PMID:6987663[5]

IGI: Inferred from Genetic Interaction

UniProtKB:P06722|UniProtKB:P23367

C

P06722 (MutH) P23367 (MutL)

complete

GO:0003684

damaged DNA binding

GOA:hamap
GO_REF:0000020

IEA: Inferred from Electronic Annotation

HAMAP:MF_00096

F

Seeded from EcoCyc (v14.0)

complete

GO:0005524

ATP binding

GOA:hamap
GO_REF:0000020

IEA: Inferred from Electronic Annotation

HAMAP:MF_00096

F

Seeded from EcoCyc (v14.0)

complete

GO:0005524

ATP binding

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR000432

F

Seeded from EcoCyc (v14.0)

complete

GO:0005524

ATP binding

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR005748

F

Seeded from EcoCyc (v14.0)

complete

GO:0005524

ATP binding

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR007695

F

Seeded from EcoCyc (v14.0)

complete

GO:0005524

ATP binding

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR007696

F

Seeded from EcoCyc (v14.0)

complete

GO:0005524

ATP binding

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR007860

F

Seeded from EcoCyc (v14.0)

complete

GO:0005524

ATP binding

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR007861

F

Seeded from EcoCyc (v14.0)

complete

GO:0005524

ATP binding

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR016151

F

Seeded from EcoCyc (v14.0)

complete

GO:0005524

ATP binding

GOA:spkw
SP_KW:GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0067

F

Seeded from EcoCyc (v14.0)

complete

GO:0006298

mismatch repair

GOA:hamap
GO_REF:0000020

IEA: Inferred from Electronic Annotation

HAMAP:MF_00096

P

Seeded from EcoCyc (v14.0)

complete

GO:0006298

mismatch repair

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR000432

P

Seeded from EcoCyc (v14.0)

complete

GO:0006298

mismatch repair

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR005748

P

Seeded from EcoCyc (v14.0)

complete

GO:0006298

mismatch repair

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR007695

P

Seeded from EcoCyc (v14.0)

complete

GO:0032136

adenine/cytosine mispair binding

PMID:11237867[9]

IDA: Inferred from Direct Assay

F

complete

GO:0006298

mismatch repair

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR007696

P

Seeded from EcoCyc (v14.0)

complete

GO:0006298

mismatch repair

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR007860

P

Seeded from EcoCyc (v14.0)

complete

GO:0006298

mismatch repair

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR007861

P

Seeded from EcoCyc (v14.0)

complete

GO:0006298

mismatch repair

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR016151

P

Seeded from EcoCyc (v14.0)

complete

GO:0030983

mismatched DNA binding

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR000432

F

Seeded from EcoCyc (v14.0)

complete

GO:0030983

mismatched DNA binding

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR005748

F

Seeded from EcoCyc (v14.0)

complete

GO:0030983

mismatched DNA binding

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR007695

F

Seeded from EcoCyc (v14.0)

complete

GO:0030983

mismatched DNA binding

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR007696

F

Seeded from EcoCyc (v14.0)

complete

GO:0030983

mismatched DNA binding

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR007860

F

Seeded from EcoCyc (v14.0)

complete

GO:0030983

mismatched DNA binding

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR007861

F

Seeded from EcoCyc (v14.0)

complete

GO:0030983

mismatched DNA binding

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR016151

F

Seeded from EcoCyc (v14.0)

complete

GO:0006974

response to DNA damage stimulus

PMID:11967071[10]

IEP: Inferred from Expression Pattern

P

complete

GO:0043531

ADP binding

PMID:11048711[11]

IDA: Inferred from Direct Assay

F

Xstal structure

complete

GO:0030983

mismatched DNA binding

PMID:11048711[11]

IDA: Inferred from Direct Assay

F

Xstal structure

complete

GO:0008301

DNA bending activity

PMID:14634210[12]

IDA: Inferred from Direct Assay

F

atomic force microscopy

complete

GO:0006298

mismatch repair

PMID:14634210[12]

IDA: Inferred from Direct Assay

P

Atomic force microscopy

complete

GO:0005524

ATP binding

PMID:12606120[13]

IDA: Inferred from Direct Assay

F

complete

GO:0030983

mismatched DNA binding

PMID:3014530[6]

IDA: Inferred from Direct Assay

F

Enzymatic and chemical protection (footprinting) assays

complete

GO:0000018

regulation of DNA recombination

PMID:2555716[14]

IMP: Inferred from Mutant Phenotype

P

complete

Interactions See Help:Product_interactions for help entering or editing information about gene product interactions in this section of EcoliWiki.

Partner Type Partner Notes References Evidence

Protein

Subunits of MutHLS complex, methyl-directed mismatch repair

PMID:6987663[5]

Inferred from genetic interaction

Protein

tufA

PMID:15690043[15]

Experiment(s):EBI-886447

Protein

galF

PMID:16606699[16]

Experiment(s):EBI-1143773

Protein

baeS

PMID:16606699[16]

Experiment(s):EBI-1143773

Protein

envZ

PMID:16606699[16]

Experiment(s):EBI-1143773

Protein

tufB

PMID:19402753[17]

MALDI(Z-score):19.762370

Protein

DnaN: beta sliding clamp subunit of DNA pol III

PMID:11459978[18]

Protein mobility shift during native gel electrophoresis and kinase protection assay.

DNA

GT mismatches

PMID:11048711[11]

Crystal structure

Protein

MutL

PMID:9250691[19]

Visualized using EM

DNA

Heteroduplex DNA

PMID:9250691[19]

Visualized using EM

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Notes

Localization

See Help:Product_localization for how to add or edit information in this section of EcoliWiki.

Compartment Description Evidence Reference/Source Notes

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Notes

Structure and Physical Properties

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<protect> Physical Properties See Help:Product_physical_properties for help entering or editing information about the physical properties of this gene product.

Name
Sequence

at EcoCyc

MSAIENFDAH TPMMQQYLRL KAQHPEILLF YRMGDFYELF YDDAKRASQL LDISLTKRGA
SAGEPIPMAG IPYHAVENYL AKLVNQGESV AICEQIGDPA TSKGPVERKV VRIVTPGTIS
DEALLQERQD NLLAAIWQDS KGFGYATLDI SSGRFRLSEP ADRETMAAEL QRTNPAELLY
AEDFAEMSLI EGRRGLRRRP LWEFEIDTAR QQLNLQFGTR DLVGFGVENA PRGLCAAGCL
LQYAKDTQRT TLPHIRSITM EREQDSIIMD AATRRNLEIT QNLAGGAENT LASVLDCTVT
PMGSRMLKRW LHMPVRDTRV LLERQQTIGA LQDFTAGLQP VLRQVGDLER ILARLALRTA
RPRDLARMRH AFQQLPELRA QLETVDSAPV QALREKMGEF AELRDLLERA IIDTPPVLVR
DGGVIASGYN EELDEWRALA DGATDYLERL EVRERERTGL DTLKVGFNAV HGYYIQISRG
QSHLAPINYM RRQTLKNAER YIIPELKEYE DKVLTSKGKA LALEKQLYEE LFDLLLPHLE
ALQQSASALA ELDVLVNLAE RAYTLNYTCP TFIDKPGIRI TEGRHPVVEQ VLNEPFIANP
LNLSPQRRML IITGPNMGGK STYMRQTALI ALMAYIGSYV PAQKVEIGPI DRIFTRVGAA
DDLASGRSTF MVEMTETANI LHNATEYSLV LMDEIGRGTS TYDGLSLAWA CAENLANKIK
ALTLFATHYF ELTQLPEKME GVANVHLDAL EHGDTIAFMH SVQDGAASKS YGLAVAALAG
VPKEVIKRAR QKLRELESIS PNAAATQVDG TQMSLLSVPE ETSPAVEALE NLDPDSLTPR
QALEWIYRLK SLV
Length

853

Mol. Wt

95.249 kDa

pI

5.4 (calculated)

Extinction coefficient

73,230 - 73,980 (calc based on 27 Y, 6 W, and 6 C residues)


Domains/Motifs/Modification Sites

See Help:Product_domains_motifs for help entering or editing information in this section of EcoliWiki.

Type Residues Description Notes References

Domain

11..123

PF01624 MutS domain I

PMID:19920124[20]

Domain

131..256

PF05188 MutS domain II

PMID:19920124[20]

Domain

264..564

PF05192 MutS domain III

PMID:19920124[20]

Domain

428..519

PF05190 MutS family domain IV

PMID:19920124[20]

Domain

567..799

PF00488 MutS domain V

PMID:19920124[20]

<motif_map/>

Structure
See Help:Product_structure for help entering or editing information in this section of EcoliWiki.

Structures

<beststructure> gene=mutS taxon=562,83333 </beststructure>

Models

View models at:

</protect>

Structure figures

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</protect>

Notes

Analytical ultracentrifugation data suggest that MutS exists as an equilibrating mixture of dimers and tetramers, both of which would be present at physiologically relevant concentrations. Kinetic parameters for ATPase activity and oligomerization are described[21][8]

There are several structure papers for MutS:

  • The crystal structure of DNA mismatch repair protein MutS binding to a G-T mismatch[11]
  • Crystal structures of mismatch repair protein MutS and its complex with a substrate DNA[22]

Gene Product Resources

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See Help:Product_resources for help with entering or editing information in this section of EcoliWiki.

Resource type Source Notes/Reference

Purification protocol

from plasmid pMS312

PMID:3014530[6]

Purification protocol

Single-step purification of His6-MutS

PMID:8747662[23]

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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

NCBI (Protein) (EcoliWiki Page)

GI:16130640

Escherichia coli str. K-12 substr. MG1655

NCBI (Protein) (EcoliWiki Page)

GeneID:947206

Escherichia coli str. K-12 substr. MG1655

ASAP

ASAP:ABE-0008977

Escherichia coli str. K-12 substr. MG1655

UniProt (EcoliWiki Page)

UniProtKB/Swiss-Prot:P23909

Escherichia coli str. K-12 substr. MG1655

EcoCyc

EcoCyc:EG10625

Escherichia coli str. K-12 substr. MG1655

EcoGene

EcoGene:EG10625

Escherichia coli str. K-12 substr. MG1655

NCBI (Gene) (EcoliWiki Page)

GeneID:947206

Escherichia coli str. K-12 substr. MG1655

RegulonDB

RegulonDB:ECK120000618

Escherichia coli str. K-12 substr. MG1655

EchoBASE

EchoBASE:EB0620

Escherichia coli str. K-12 substr. MG1655

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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. 1.0 1.1 1.2 1.3 1.4 1.5 Riley, M. et al. (2006) Nucleic Acids Res 34:1-6 (corrected supplemental data from B. Wanner)
  2. 2.0 2.1 2.2 2.3 2.4 2.5 2.6 EcoCyc (release 10.6; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
  3. 3.0 3.1 EcoCyc (release 11.1; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
  4. EcoGene: Rudd, KE (2000) EcoGene: a genome sequence database for Escherichia coli K-12. Nucleic Acids Res 28:60-4.
  5. 5.0 5.1 5.2 Glickman, BW & Radman, M (1980) Escherichia coli mutator mutants deficient in methylation-instructed DNA mismatch correction. Proc. Natl. Acad. Sci. U.S.A. 77 1063-7 PubMed
  6. 6.0 6.1 6.2 Su, SS & Modrich, P (1986) Escherichia coli mutS-encoded protein binds to mismatched DNA base pairs. Proc. Natl. Acad. Sci. U.S.A. 83 5057-61 PubMed
  7. Lahue, RS et al. (1989) DNA mismatch correction in a defined system. Science 245 160-4 PubMed
  8. 8.0 8.1 Bjornson, KP et al. (2000) Modulation of MutS ATP hydrolysis by DNA cofactors. Biochemistry 39 3176-83 PubMed
  9. Brown, J et al. (2001) Affinity of mismatch-binding protein MutS for heteroduplexes containing different mismatches. Biochem. J. 354 627-33 PubMed
  10. Khil, PP & Camerini-Otero, RD (2002) Over 1000 genes are involved in the DNA damage response of Escherichia coli. Mol. Microbiol. 44 89-105 PubMed
  11. 11.0 11.1 11.2 11.3 Lamers, MH et al. (2000) The crystal structure of DNA mismatch repair protein MutS binding to a G x T mismatch. Nature 407 711-7 PubMed
  12. 12.0 12.1 Wang, H et al. (2003) DNA bending and unbending by MutS govern mismatch recognition and specificity. Proc. Natl. Acad. Sci. U.S.A. 100 14822-7 PubMed
  13. 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
  14. Rayssiguier, C et al. (1989) The barrier to recombination between Escherichia coli and Salmonella typhimurium is disrupted in mismatch-repair mutants. Nature 342 396-401 PubMed
  15. Butland, G et al. (2005) Interaction network containing conserved and essential protein complexes in Escherichia coli. Nature 433 531-7 PubMed
  16. 16.0 16.1 16.2 Arifuzzaman, M et al. (2006) Large-scale identification of protein-protein interaction of Escherichia coli K-12. Genome Res. 16 686-91 PubMed
  17. Hu, P et al. (2009) Global functional atlas of Escherichia coli encompassing previously uncharacterized proteins. PLoS Biol. 7 e96 PubMed
  18. López de Saro, FJ & O'Donnell, M (2001) Interaction of the beta sliding clamp with MutS, ligase, and DNA polymerase I. Proc. Natl. Acad. Sci. U.S.A. 98 8376-80 PubMed
  19. 19.0 19.1 Allen, DJ et al. (1997) MutS mediates heteroduplex loop formation by a translocation mechanism. EMBO J. 16 4467-76 PubMed
  20. 20.0 20.1 20.2 20.3 20.4 Finn, RD et al. (2010) The Pfam protein families database. Nucleic Acids Res. 38 D211-22 PubMed
  21. Bjornson, KP et al. (2003) Assembly and molecular activities of the MutS tetramer. J. Biol. Chem. 278 34667-73 PubMed
  22. Obmolova, G et al. (2000) Crystal structures of mismatch repair protein MutS and its complex with a substrate DNA. Nature 407 703-10 PubMed
  23. Feng, G & Winkler, ME (1995) Single-step purifications of His6-MutH, His6-MutL and His6-MutS repair proteins of escherichia coli K-12. BioTechniques 19 956-65 PubMed

Categories

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