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P25847

- MSH2_YEAST

UniProt

P25847 - MSH2_YEAST

Protein

DNA mismatch repair protein MSH2

Gene

MSH2

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 133 (01 Oct 2014)
      Sequence version 2 (01 Nov 1997)
      Previous versions | rss
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    Functioni

    Component of the post-replicative DNA mismatch repair system (MMR). Forms two different heterodimers: MutS alpha (MSH2-MSH6 heterodimer) and MutS beta (MSH2-MSH3 heterodimer), which bind to DNA mismatches thereby initiating DNA repair. MSH2 seems to act as a scaffold for the other MutS homologs that provide substrate-binding and substrate specificity. When bound, heterodimers bend the DNA helix and shield approximately 20 base pairs. MutS alpha acts mainly to repair base-base and single insertion-deletion mismatches that occur during replication, but can also repair longer insertion-deletion loops (IDLs), although with decreasing efficiency as the size of the extrahelical loop increases. MutS beta acts mainly to repair IDLs from 2 to 13 nucleotides in size, but can also repair base-base and single insertion-deletion mismatches. After mismatch binding, MutS alpha or beta form a ternary complex with a MutL heterodimer, which is thought to be responsible for directing the downstream MMR events, including strand discrimination, excision, and resynthesis. ATP binding and hydrolysis play a pivotal role in mismatch repair functions. Both subunits bind ATP, but with differing affinities, and their ATPase kinetics are also very different. MSH6 binds and hydrolyzes ATP rapidly, whereas MSH2 catalyzes ATP at a substantially slower rate. Binding to a mismatched base pair suppresses MSH6-catalyzed ATP hydrolysis, but not the activity of MSH2. ATP binding to both subunits is necessary to trigger a change in MutS alpha interaction with mismatched DNA, converting MutS alpha into a sliding clamp capable of hydrolysis-independent movement along DNA, and also facilitates formation of ternary complexes containing MutS and MutL proteins and the mismatch. MutS beta also has a role in regulation of heteroduplex formation during mitotic and meiotic recombination. MutS beta binds to DNA flap structures predicted to form during recombination, and is required for 3' non-homologous tail removal (NHTR). MutS beta-binding alters the DNA conformation of its substrate at the ds/ssDNA junction and may facilitate its recognition and/or cleavage by the downstream nucleotide excision repair (NER) RAD1-RAD10 endonuclease.19 Publications

    Enzyme regulationi

    Inhibited by Cd2+.2 Publications

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi688 – 6958ATPSequence Analysis

    GO - Molecular functioni

    1. ATPase activity Source: SGD
    2. ATP binding Source: SGD
    3. double-strand/single-strand DNA junction binding Source: SGD
    4. four-way junction DNA binding Source: SGD
    5. mismatched DNA binding Source: InterPro
    6. protein binding Source: IntAct

    GO - Biological processi

    1. ATP catabolic process Source: GOC
    2. chromatin silencing at silent mating-type cassette Source: SGD
    3. DNA recombination Source: SGD
    4. interstrand cross-link repair Source: SGD
    5. meiotic gene conversion Source: SGD
    6. meiotic mismatch repair Source: SGD
    7. mismatch repair Source: SGD
    8. mitotic recombination Source: SGD
    9. removal of nonhomologous ends Source: SGD

    Keywords - Biological processi

    DNA damage, DNA repair

    Keywords - Ligandi

    ATP-binding, DNA-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciYEAST:G3O-33490-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    DNA mismatch repair protein MSH2
    Alternative name(s):
    MutS protein homolog 2
    Gene namesi
    Name:MSH2
    Ordered Locus Names:YOL090W
    ORF Names:O0935
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome XV

    Organism-specific databases

    CYGDiYOL090w.
    SGDiS000005450. MSH2.

    Subcellular locationi

    Nucleus 1 Publication

    GO - Cellular componenti

    1. MutSalpha complex Source: SGD
    2. MutSbeta complex Source: SGD
    3. nuclear chromosome Source: SGD

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi42 – 421Y → A: Moderately reduced activity in a mismatch repair assay. 2 Publications
    Mutagenesisi65 – 651K → A: Defective in a mismatch repair assay. 2 Publications
    Mutagenesisi317 – 3171G → D: Partially defective in a mismatch repair assay. 3 Publications
    Mutagenesisi402 – 4021L → F: Partially defective in a mismatch repair assay. 2 Publications
    Mutagenesisi430 – 4301Q → K: Partially defective in a mismatch repair assay. 2 Publications
    Mutagenesisi518 – 5181A → P: Defective in MMR, but not in NHTR. 1 Publication
    Mutagenesisi524 – 5241D → Y: Partially defective in a mismatch repair assay. 2 Publications
    Mutagenesisi542 – 5421R → P: Defective in a mismatch repair assay. 2 Publications
    Mutagenesisi561 – 5611S → P: Causes strong defects in MutS alpha mismatch binding. Defective in MMR, but not in NHTR. 2 Publications
    Mutagenesisi564 – 5641K → E: Causes strong defects in MutS alpha mismatch binding. Defective in MMR, but not in NHTR. 2 Publications
    Mutagenesisi566 – 5661G → D: Defective in MMR, but not in NHTR. 2 Publications
    Mutagenesisi574 – 5741L → S: Defective in MMR and in NHTR. 1 Publication
    Mutagenesisi584 – 5841L → P: Defective in MMR and in NHTR. 1 Publication
    Mutagenesisi640 – 6401P → L: Defective in a mismatch repair assay. 3 Publications
    Mutagenesisi656 – 6561S → P: Causes defects in ATP-dependent dissociation of MutS alpha from mismatch DNA and in interactions between MutS alpha and MutL alpha. Defective in MMR, but not in NHTR. 2 Publications
    Mutagenesisi658 – 6581H → Y: Fully functional in a mismatch repair assay. 2 Publications
    Mutagenesisi688 – 6881G → A: Moderately reduced activity in a mismatch repair assay. 2 Publications
    Mutagenesisi693 – 6931G → A or S: Has a dominant negative mutator effect. 3 Publications
    Mutagenesisi693 – 6931G → D: Has no defect in mismatch DNA binding, but lacks ATP-induced conformational change. Defective in MMR and in NHTR. 3 Publications
    Mutagenesisi694 – 6941K → A: Impairs ATP binding; reduces catalytic activity 1.6-fold for ATP hydrolysis. Has a dominant negative mutator effect. 4 Publications
    Mutagenesisi694 – 6941K → R: Defective in MMR and in NHTR. 4 Publications
    Mutagenesisi695 – 6951S → A: Has a dominant negative mutator effect. 2 Publications
    Mutagenesisi716 – 7161C → F: Defective in a mismatch repair assay. 2 Publications
    Mutagenesisi730 – 7301R → W: Disruptes MutS alpha ATPase activity, but does not affect ATP binding or interactions with MutL alpha. Defective in MMR, but not in NHTR. 2 Publications
    Mutagenesisi742 – 7421S → F: Defective in MMR, but not in NHTR. 1 Publication
    Mutagenesisi742 – 7421S → P: Defective in MMR and in NHTR. 1 Publication
    Mutagenesisi768 – 7681E → A: Reduces catalytic activity 50-fold for ATP hydrolysis. 4 Publications
    Mutagenesisi773 – 7731T → I: Defective in MMR and in NHTR. 1 Publication
    Mutagenesisi855 – 8551G → D: Defective in MMR, but not in NHTR. 1 Publication
    Mutagenesisi859 – 8591A → E: Defective in MMR, but not in NHTR. 1 Publication
    Mutagenesisi862 – 8621V → D: Defective in MMR, but not in NHTR. 1 Publication
    Mutagenesisi863 – 8686Missing: Defective in MMR and in NHTR. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 964964DNA mismatch repair protein MSH2PRO_0000115191Add
    BLAST

    Proteomic databases

    MaxQBiP25847.
    PaxDbiP25847.
    PeptideAtlasiP25847.

    Expressioni

    Gene expression databases

    GenevestigatoriP25847.

    Interactioni

    Subunit structurei

    Heterodimer consisting of MSH2-MSH6 (MutS alpha) or MSH2-MSH3 (MutS beta). Both heterodimers form a ternary complex with MutL alpha (MLH1-PMS1). MutS beta also forms a ternary complex with MutL beta (MLH1-MLH3), and possibly with a MLH1-MLH2 heterodimer. Both heterodimers interact with proliferating cell nuclear antigen (PCNA/POL30). This interaction is disrupted upon binding of the MutS heterodimers to mismatch DNA. Interacts with SAW1.7 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    EXO1P398753EBI-11352,EBI-6738
    MSH3P253363EBI-11352,EBI-11362
    MSH6Q038346EBI-11352,EBI-11383

    Protein-protein interaction databases

    BioGridi34312. 138 interactions.
    DIPiDIP-2415N.
    IntActiP25847. 35 interactions.
    MINTiMINT-631153.
    STRINGi4932.YOL090W.

    Structurei

    3D structure databases

    ProteinModelPortaliP25847.
    SMRiP25847. Positions 14-913.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni851 – 964114Interaction with MSH6Add
    BLAST

    Sequence similaritiesi

    Belongs to the DNA mismatch repair MutS family.Curated

    Phylogenomic databases

    eggNOGiCOG0249.
    GeneTreeiENSGT00550000074867.
    HOGENOMiHOG000196498.
    KOiK08735.
    OMAiLNKCRTP.
    OrthoDBiEOG773XQH.

    Family and domain databases

    Gene3Di3.30.420.110. 1 hit.
    3.40.50.300. 1 hit.
    InterProiIPR011184. DNA_mismatch_repair_MSH2.
    IPR007695. DNA_mismatch_repair_MutS-lik_N.
    IPR000432. DNA_mismatch_repair_MutS_C.
    IPR007861. DNA_mismatch_repair_MutS_clamp.
    IPR007696. DNA_mismatch_repair_MutS_core.
    IPR007860. DNA_mmatch_repair_MutS_con_dom.
    IPR027417. P-loop_NTPase.
    [Graphical view]
    PfamiPF01624. MutS_I. 1 hit.
    PF05188. MutS_II. 1 hit.
    PF05192. MutS_III. 1 hit.
    PF05190. MutS_IV. 1 hit.
    PF00488. MutS_V. 1 hit.
    [Graphical view]
    PIRSFiPIRSF005813. MSH2. 1 hit.
    SMARTiSM00534. MUTSac. 1 hit.
    SM00533. MUTSd. 1 hit.
    [Graphical view]
    SUPFAMiSSF48334. SSF48334. 1 hit.
    SSF52540. SSF52540. 1 hit.
    PROSITEiPS00486. DNA_MISMATCH_REPAIR_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P25847-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSSTRPELKF SDVSEERNFY KKYTGLPKKP LKTIRLVDKG DYYTVIGSDA    50
    IFVADSVYHT QSVLKNCQLD PVTAKNFHEP TKYVTVSLQV LATLLKLCLL 100
    DLGYKVEIYD KGWKLIKSAS PGNIEQVNEL MNMNIDSSII IASLKVQWNS 150
    QDGNCIIGVA FIDTTAYKVG MLDIVDNEVY SNLESFLIQL GVKECLVQDL 200
    TSNSNSNAEM QKVINVIDRC GCVVTLLKNS EFSEKDVELD LTKLLGDDLA 250
    LSLPQKYSKL SMGACNALIG YLQLLSEQDQ VGKYELVEHK LKEFMKLDAS 300
    AIKALNLFPQ GPQNPFGSNN LAVSGFTSAG NSGKVTSLFQ LLNHCKTNAG 350
    VRLLNEWLKQ PLTNIDEINK RHDLVDYLID QIELRQMLTS EYLPMIPDIR 400
    RLTKKLNKRG NLEDVLKIYQ FSKRIPEIVQ VFTSFLEDDS PTEPVNELVR 450
    SVWLAPLSHH VEPLSKFEEM VETTVDLDAY EENNEFMIKV EFNEELGKIR 500
    SKLDTLRDEI HSIHLDSAED LGFDPDKKLK LENHHLHGWC MRLTRNDAKE 550
    LRKHKKYIEL STVKAGIFFS TKQLKSIANE TNILQKEYDK QQSALVREII 600
    NITLTYTPVF EKLSLVLAHL DVIASFAHTS SYAPIPYIRP KLHPMDSERR 650
    THLISSRHPV LEMQDDISFI SNDVTLESGK GDFLIITGPN MGGKSTYIRQ 700
    VGVISLMAQI GCFVPCEEAE IAIVDAILCR VGAGDSQLKG VSTFMVEILE 750
    TASILKNASK NSLIIVDELG RGTSTYDGFG LAWAIAEHIA SKIGCFALFA 800
    THFHELTELS EKLPNVKNMH VVAHIEKNLK EQKHDDEDIT LLYKVEPGIS 850
    DQSFGIHVAE VVQFPEKIVK MAKRKANELD DLKTNNEDLK KAKLSLQEVN 900
    EGNIRLKALL KEWIRKVKEE GLHDPSKITE EASQHKIQEL LRAIANEPEK 950
    ENDNYLKYIK ALLL 964
    Length:964
    Mass (Da):108,884
    Last modified:November 1, 1997 - v2
    Checksum:i43FFD8A640138AE4
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti957 – 9648KYIKALLL → EIYKSPCCYN in AAA34802. (PubMed:1459447)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M84170 Genomic DNA. Translation: AAA34802.1.
    X83121 Genomic DNA. Translation: CAA58189.1.
    Z74832 Genomic DNA. Translation: CAA99102.1.
    BK006948 Genomic DNA. Translation: DAA10694.1.
    PIRiS57379.
    RefSeqiNP_014551.1. NM_001183344.1.

    Genome annotation databases

    EnsemblFungiiYOL090W; YOL090W; YOL090W.
    GeneIDi854063.
    KEGGisce:YOL090W.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M84170 Genomic DNA. Translation: AAA34802.1 .
    X83121 Genomic DNA. Translation: CAA58189.1 .
    Z74832 Genomic DNA. Translation: CAA99102.1 .
    BK006948 Genomic DNA. Translation: DAA10694.1 .
    PIRi S57379.
    RefSeqi NP_014551.1. NM_001183344.1.

    3D structure databases

    ProteinModelPortali P25847.
    SMRi P25847. Positions 14-913.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 34312. 138 interactions.
    DIPi DIP-2415N.
    IntActi P25847. 35 interactions.
    MINTi MINT-631153.
    STRINGi 4932.YOL090W.

    Proteomic databases

    MaxQBi P25847.
    PaxDbi P25847.
    PeptideAtlasi P25847.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YOL090W ; YOL090W ; YOL090W .
    GeneIDi 854063.
    KEGGi sce:YOL090W.

    Organism-specific databases

    CYGDi YOL090w.
    SGDi S000005450. MSH2.

    Phylogenomic databases

    eggNOGi COG0249.
    GeneTreei ENSGT00550000074867.
    HOGENOMi HOG000196498.
    KOi K08735.
    OMAi LNKCRTP.
    OrthoDBi EOG773XQH.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-33490-MONOMER.

    Miscellaneous databases

    NextBioi 975668.
    PROi P25847.

    Gene expression databases

    Genevestigatori P25847.

    Family and domain databases

    Gene3Di 3.30.420.110. 1 hit.
    3.40.50.300. 1 hit.
    InterProi IPR011184. DNA_mismatch_repair_MSH2.
    IPR007695. DNA_mismatch_repair_MutS-lik_N.
    IPR000432. DNA_mismatch_repair_MutS_C.
    IPR007861. DNA_mismatch_repair_MutS_clamp.
    IPR007696. DNA_mismatch_repair_MutS_core.
    IPR007860. DNA_mmatch_repair_MutS_con_dom.
    IPR027417. P-loop_NTPase.
    [Graphical view ]
    Pfami PF01624. MutS_I. 1 hit.
    PF05188. MutS_II. 1 hit.
    PF05192. MutS_III. 1 hit.
    PF05190. MutS_IV. 1 hit.
    PF00488. MutS_V. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF005813. MSH2. 1 hit.
    SMARTi SM00534. MUTSac. 1 hit.
    SM00533. MUTSd. 1 hit.
    [Graphical view ]
    SUPFAMi SSF48334. SSF48334. 1 hit.
    SSF52540. SSF52540. 1 hit.
    PROSITEi PS00486. DNA_MISMATCH_REPAIR_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Isolation and characterization of two Saccharomyces cerevisiae genes encoding homologs of the bacterial HexA and MutS mismatch repair proteins."
      Reenan R.A.G., Kolodner R.D.
      Genetics 132:963-973(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "A 29.425 kb segment on the left arm of yeast chromosome XV contains more than twice as many unknown as known open reading frames."
      Zumstein E., Pearson B.M., Kalogeropoulos A., Schweizer M.
      Yeast 11:975-986(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 96604 / S288c / FY1679.
    3. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV."
      Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J., Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A., Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B., Dang V.-D.
      , de Haan M., Delius H., Durand P., Fairhead C., Feldmann H., Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U., Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B., Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A., Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C., Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G., Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B., Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F., Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E., Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.
      Nature 387:98-102(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    4. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    5. "Characterization of insertion mutations in the Saccharomyces cerevisiae MSH1 and MSH2 genes: evidence for separate mitochondrial and nuclear functions."
      Reenan R.A.G., Kolodner R.D.
      Genetics 132:975-985(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION.
    6. "MLH1, PMS1, and MSH2 interactions during the initiation of DNA mismatch repair in yeast."
      Prolla T.A., Pang Q., Alani E., Kolodner R.D., Liskay R.M.
      Science 265:1091-1093(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: COMPLEX FORMATION WITH MLH1-PMS1.
    7. "Requirement for PCNA in DNA mismatch repair at a step preceding DNA resynthesis."
      Umar A., Buermeyer A.B., Simon J.A., Thomas D.C., Clark A.B., Liskay R.M., Kunkel T.A.
      Cell 87:65-73(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH POL30.
    8. "Binding of insertion/deletion DNA mismatches by the heterodimer of yeast mismatch repair proteins MSH2 and MSH3."
      Habraken Y., Sung P., Prakash L., Prakash S.
      Curr. Biol. 6:1185-1187(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: DNA-BINDING SPECIFICITY, INTERACTION WITH MSH3.
    9. "Redundancy of Saccharomyces cerevisiae MSH3 and MSH6 in MSH2-dependent mismatch repair."
      Marsischky G.T., Filosi N., Kane M.F., Kolodner R.D.
      Genes Dev. 10:407-420(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH MSH3 AND MSH6.
    10. "The Saccharomyces cerevisiae Msh2 and Msh6 proteins form a complex that specifically binds to duplex oligonucleotides containing mismatched DNA base pairs."
      Alani E.
      Mol. Cell. Biol. 16:5604-5615(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION, INTERACTION WITH MSH6.
    11. "Enhancement of MSH2-MSH3-mediated mismatch recognition by the yeast MLH1-PMS1 complex."
      Habraken Y., Sung P., Prakash L., Prakash S.
      Curr. Biol. 7:790-793(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DNA-BINDING SPECIFICITY, COMPLEX FORMATION WITH MLH1-PMS1.
    12. "Microsatellite instability in yeast: dependence on repeat unit size and DNA mismatch repair genes."
      Sia E.A., Kokoska R.J., Dominska M., Greenwell P., Petes T.D.
      Mol. Cell. Biol. 17:2851-2858(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN MMR.
    13. "Role of Saccharomyces cerevisiae Msh2 and Msh3 repair proteins in double-strand break-induced recombination."
      Sugawara N., Paques F., Colaiacovo M., Haber J.E.
      Proc. Natl. Acad. Sci. U.S.A. 94:9214-9219(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN NHTR.
    14. "ATP-dependent assembly of a ternary complex consisting of a DNA mismatch and the yeast MSH2-MSH6 and MLH1-PMS1 protein complexes."
      Habraken Y., Sung P., Prakash L., Prakash S.
      J. Biol. Chem. 273:9837-9841(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DNA-BINDING, COMPLEX FORMATION WITH MLH1-PMS1.
    15. "Saccharomyces cerevisiae Msh2p and Msh6p ATPase activities are both required during mismatch repair."
      Studamire B., Quach T., Alani E.
      Mol. Cell. Biol. 18:7590-7601(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF GLY-693.
    16. "The Saccharomyces cerevisiae MLH3 gene functions in MSH3-dependent suppression of frameshift mutations."
      Flores-Rozas H., Kolodner R.D.
      Proc. Natl. Acad. Sci. U.S.A. 95:12404-12409(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    17. "Mutator phenotypes of common polymorphisms and missense mutations in MSH2."
      Drotschmann K., Clark A.B., Kunkel T.A.
      Curr. Biol. 9:907-910(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF GLY-317; LEU-402; GLN-430; ASP-524; ARG-542; PRO-640 AND CYS-716.
    18. "Saccharomyces cerevisiae MSH2/6 complex interacts with Holliday junctions and facilitates their cleavage by phage resolution enzymes."
      Marsischky G.T., Lee S., Griffith J., Kolodner R.D.
      J. Biol. Chem. 274:7200-7206(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: DNA-BINDING SPECIFICITY.
    19. "Biochemical characterization of the interaction between the Saccharomyces cerevisiae MSH2-MSH6 complex and mispaired bases in DNA."
      Marsischky G.T., Kolodner R.D.
      J. Biol. Chem. 274:26668-26682(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: DNA-BINDING SPECIFICITY.
    20. "MSH2 and MSH6 are required for removal of adenine misincorporated opposite 8-oxo-guanine in S. cerevisiae."
      Ni T.T., Marsischky G.T., Kolodner R.D.
      Mol. Cell 4:439-444(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    21. "Separation-of-function mutations in Saccharomyces cerevisiae MSH2 that confer mismatch repair defects but do not affect nonhomologous-tail removal during recombination."
      Studamire B., Price G., Sugawara N., Haber J.E., Alani E.
      Mol. Cell. Biol. 19:7558-7567(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS.
    22. "Mutator phenotypes of yeast strains heterozygous for mutations in the MSH2 gene."
      Drotschmann K., Clark A.B., Tran H.T., Resnick M.A., Gordenin D.A., Kunkel T.A.
      Proc. Natl. Acad. Sci. U.S.A. 96:2970-2975(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF GLY-688; GLY-693; LYS-694 AND SER-695.
    23. "Functional interaction of proliferating cell nuclear antigen with MSH2-MSH6 and MSH2-MSH3 complexes."
      Clark A.B., Valle F., Drotschmann K., Gary R.K., Kunkel T.A.
      J. Biol. Chem. 275:36498-36501(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH POL30.
    24. "Functional analysis of human MLH1 and MSH2 missense variants and hybrid human-yeast MLH1 proteins in Saccharomyces cerevisiae."
      Ellison A.R., Lofing J., Bitter G.A.
      Hum. Mol. Genet. 10:1889-1900(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF GLY-317; PRO-640 AND HIS-658.
    25. "Asymmetric recognition of DNA local distortion. Structure-based functional studies of eukaryotic Msh2-Msh6."
      Drotschmann K., Yang W., Brownewell F.E., Kool E.T., Kunkel T.A.
      J. Biol. Chem. 276:46225-46229(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: DNA-BINDING, MUTAGENESIS OF TYR-42 AND LYS-65.
    26. "MSH-MLH complexes formed at a DNA mismatch are disrupted by the PCNA sliding clamp."
      Bowers J., Tran P.T., Joshi A., Liskay R.M., Alani E.
      J. Mol. Biol. 306:957-968(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, COMPLEX FORMATION WITH MLH1-PMS1.
    27. "Evidence for sequential action of two ATPase active sites in yeast Msh2-Msh6."
      Drotschmann K., Yang W., Kunkel T.A.
      DNA Repair 1:743-753(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF GLU-768.
    28. "Mismatch recognition-coupled stabilization of Msh2-Msh6 in an ATP-bound state at the initiation of DNA repair."
      Antony E., Hingorani M.M.
      Biochemistry 42:7682-7693(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    29. "Transfer of the MSH2.MSH6 complex from proliferating cell nuclear antigen to mispaired bases in DNA."
      Lau P.J., Kolodner R.D.
      J. Biol. Chem. 278:14-17(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH POL30.
    30. "Msh2 separation of function mutations confer defects in the initiation steps of mismatch repair."
      Kijas A.W., Studamire B., Alani E.
      J. Mol. Biol. 331:123-138(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF SER-561; LYS-564; GLY-566; SER-656 AND ARG-730.
    31. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    32. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    33. "Cadmium inhibits the functions of eukaryotic MutS complexes."
      Clark A.B., Kunkel T.A.
      J. Biol. Chem. 279:53903-53906(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME REGULATION, MUTAGENESIS OF GLU-768.
    34. "Analysis of the interaction between the Saccharomyces cerevisiae MSH2-MSH6 and MLH1-PMS1 complexes with DNA using a reversible DNA end-blocking system."
      Mendillo M.L., Mazur D.J., Kolodner R.D.
      J. Biol. Chem. 280:22245-22257(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, COMPLEX FORMATION WITH MLH1-PMS1.
    35. "Detection of high-affinity and sliding clamp modes for MSH2-MSH6 by single-molecule unzipping force analysis."
      Jiang J., Bai L., Surtees J.A., Gemici Z., Wang M.D., Alani E.
      Mol. Cell 20:771-781(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    36. "Cadmium inhibits mismatch repair by blocking the ATPase activity of the MSH2-MSH6 complex."
      Banerjee S., Flores-Rozas H.
      Nucleic Acids Res. 33:1410-1419(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME REGULATION.
    37. "Contribution of Msh2 and Msh6 subunits to the asymmetric ATPase and DNA mismatch binding activities of Saccharomyces cerevisiae Msh2-Msh6 mismatch repair protein."
      Antony E., Khubchandani S., Chen S., Hingorani M.M.
      DNA Repair 5:153-162(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF LYS-694 AND GLU-768.
    38. "Analysis of the proteins involved in the in vivo repair of base-base mismatches and four-base loops formed during meiotic recombination in the yeast Saccharomyces cerevisiae."
      Stone J.E., Petes T.D.
      Genetics 173:1223-1239(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    39. "Inhibition of Msh6 ATPase activity by mispaired DNA induces a Msh2(ATP)-Msh6(ATP) state capable of hydrolysis-independent movement along DNA."
      Mazur D.J., Mendillo M.L., Kolodner R.D.
      Mol. Cell 22:39-49(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF LYS-694.
    40. "Mismatch repair factor MSH2-MSH3 binds and alters the conformation of branched DNA structures predicted to form during genetic recombination."
      Surtees J.A., Alani E.
      J. Mol. Biol. 360:523-536(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN NHTR, DNA-BINDING.
    41. "Saccharomyces cerevisiae MSH2-MSH3 and MSH2-MSH6 complexes display distinct requirements for DNA binding domain I in mismatch recognition."
      Lee S.D., Surtees J.A., Alani E.
      J. Mol. Biol. 366:53-66(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DNA-BINDING.
    42. "Saccharomyces cerevisiae Msh2-Msh3 acts in repair of base-base mispairs."
      Harrington J.M., Kolodner R.D.
      Mol. Cell. Biol. 27:6546-6554(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    43. "Microarray-based genetic screen defines SAW1, a gene required for Rad1/Rad10-dependent processing of recombination intermediates."
      Li F., Dong J., Pan X., Oum J.-H., Boeke J.D., Lee S.E.
      Mol. Cell 30:325-335(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SAW1.

    Entry informationi

    Entry nameiMSH2_YEAST
    AccessioniPrimary (citable) accession number: P25847
    Secondary accession number(s): D6W1X8, Q12423
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 1, 1992
    Last sequence update: November 1, 1997
    Last modified: October 1, 2014
    This is version 133 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Present with 1230 molecules/cell in log phase SD medium.1 Publication

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families
    2. Yeast
      Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
    3. Yeast chromosome XV
      Yeast (Saccharomyces cerevisiae) chromosome XV: entries and gene names

    External Data

    Dasty 3