MSH1_YEAST
ID MSH1_YEAST Reviewed; 959 AA.
AC P25846; D3DL70;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 2.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=DNA mismatch repair protein MSH1, mitochondrial;
DE AltName: Full=MutS protein homolog 1;
DE Flags: Precursor;
GN Name=MSH1; OrderedLocusNames=YHR120W;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1459447; DOI=10.1093/genetics/132.4.963;
RA Reenan R.A.G., Kolodner R.D.;
RT "Isolation and characterization of two Saccharomyces cerevisiae genes
RT encoding homologs of the bacterial HexA and MutS mismatch repair
RT proteins.";
RL Genetics 132:963-973(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8091229; DOI=10.1126/science.8091229;
RA Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J., Du Z.,
RA Favello A., Fulton L., Gattung S., Geisel C., Kirsten J., Kucaba T.,
RA Hillier L.W., Jier M., Johnston L., Langston Y., Latreille P., Louis E.J.,
RA Macri C., Mardis E., Menezes S., Mouser L., Nhan M., Rifkin L., Riles L.,
RA St Peter H., Trevaskis E., Vaughan K., Vignati D., Wilcox L., Wohldman P.,
RA Waterston R., Wilson R., Vaudin M.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome
RT VIII.";
RL Science 265:2077-2082(1994).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP PROTEIN SEQUENCE OF 22-31, FUNCTION, SUBCELLULAR LOCATION, AND DNA-BINDING.
RX PubMed=7961998; DOI=10.1016/s0021-9258(18)43978-6;
RA Chi N.-W., Kolodner R.D.;
RT "Purification and characterization of MSH1, a yeast mitochondrial protein
RT that binds to DNA mismatches.";
RL J. Biol. Chem. 269:29984-29992(1994).
RN [5]
RP CHARACTERIZATION.
RX PubMed=1334021; DOI=10.1093/genetics/132.4.975;
RA Reenan R.A.G., Kolodner R.D.;
RT "Characterization of insertion mutations in the Saccharomyces cerevisiae
RT MSH1 and MSH2 genes: evidence for separate mitochondrial and nuclear
RT functions.";
RL Genetics 132:975-985(1992).
RN [6]
RP FUNCTION.
RX PubMed=7961999; DOI=10.1016/s0021-9258(18)43979-8;
RA Chi N.-W., Kolodner R.D.;
RT "The effect of DNA mismatches on the ATPase activity of MSH1, a protein in
RT yeast mitochondria that recognizes DNA mismatches.";
RL J. Biol. Chem. 269:29993-29997(1994).
RN [7]
RP FUNCTION.
RX PubMed=9726974; DOI=10.1074/jbc.273.37.23690;
RA Vanderstraeten S., Van den Brule S., Hu J., Foury F.;
RT "The role of 3'-5' exonucleolytic proofreading and mismatch repair in yeast
RT mitochondrial DNA error avoidance.";
RL J. Biol. Chem. 273:23690-23697(1998).
RN [8]
RP FUNCTION, AND MUTAGENESIS OF GLY-776 AND ARG-813.
RX PubMed=11862493; DOI=10.1007/s00438-001-0621-x;
RA Koprowski P., Fikus M.U., Mieczkowski P., Ciesla Z.;
RT "A dominant mitochondrial mutator phenotype of Saccharomyces cerevisiae
RT conferred by msh1 alleles altered in the sequence encoding the ATP-binding
RT domain.";
RL Mol. Genet. Genomics 266:988-994(2002).
RN [9]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [10]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [11]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 76625 / YPH499;
RX PubMed=14576278; DOI=10.1073/pnas.2135385100;
RA Sickmann A., Reinders J., Wagner Y., Joppich C., Zahedi R.P., Meyer H.E.,
RA Schoenfisch B., Perschil I., Chacinska A., Guiard B., Rehling P.,
RA Pfanner N., Meisinger C.;
RT "The proteome of Saccharomyces cerevisiae mitochondria.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:13207-13212(2003).
RN [12]
RP FUNCTION.
RX PubMed=15010316; DOI=10.1016/j.dnarep.2003.12.005;
RA Dzierzbicki P., Koprowski P., Fikus M.U., Malc E., Ciesla Z.;
RT "Repair of oxidative damage in mitochondrial DNA of Saccharomyces
RT cerevisiae: involvement of the MSH1-dependent pathway.";
RL DNA Repair 3:403-411(2004).
RN [13]
RP FUNCTION, MUTAGENESIS OF PHE-105 AND GLY-776, AND SUBCELLULAR LOCATION.
RX PubMed=15611870; DOI=10.1007/s00294-004-0537-1;
RA Mookerjee S.A., Lyon H.D., Sia E.A.;
RT "Analysis of the functional domains of the mismatch repair homologue Msh1p
RT and its role in mitochondrial genome maintenance.";
RL Curr. Genet. 47:84-99(2005).
RN [14]
RP FUNCTION, AND MUTAGENESIS OF PHE-105; GLY-776 AND ARG-813.
RX PubMed=16337661; DOI=10.1016/j.mrfmmm.2005.10.006;
RA Mookerjee S.A., Sia E.A.;
RT "Overlapping contributions of Msh1p and putative recombination proteins
RT Cce1p, Din7p, and Mhr1p in large-scale recombination and genome sorting
RT events in the mitochondrial genome of Saccharomyces cerevisiae.";
RL Mutat. Res. 595:91-106(2006).
CC -!- FUNCTION: Important for mitochondrial DNA (mtDNA) stability and repair.
CC Recognizes and binds to base-base and small insertion-deletion
CC mismatches in mtDNA. ATP binding and hydrolysis is crucial for
CC function. Binding to a mismatched base pair attenuates ATP hydrolysis.
CC Also involved in proper sorting of mtDNA during mtDNA transmission.
CC {ECO:0000269|PubMed:11862493, ECO:0000269|PubMed:15010316,
CC ECO:0000269|PubMed:15611870, ECO:0000269|PubMed:16337661,
CC ECO:0000269|PubMed:7961998, ECO:0000269|PubMed:7961999,
CC ECO:0000269|PubMed:9726974}.
CC -!- SUBUNIT: Homodimer. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:14576278, ECO:0000269|PubMed:15611870,
CC ECO:0000269|PubMed:7961998}.
CC -!- MISCELLANEOUS: Present with 1670 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the DNA mismatch repair MutS family.
CC {ECO:0000305}.
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DR EMBL; M84169; AAA34801.1; -; Genomic_DNA.
DR EMBL; U00059; AAB68849.1; -; Genomic_DNA.
DR EMBL; BK006934; DAA06814.1; -; Genomic_DNA.
DR PIR; S48962; S48962.
DR RefSeq; NP_011988.1; NM_001179250.1.
DR AlphaFoldDB; P25846; -.
DR SMR; P25846; -.
DR BioGRID; 36553; 141.
DR DIP; DIP-6433N; -.
DR IntAct; P25846; 12.
DR STRING; 4932.YHR120W; -.
DR iPTMnet; P25846; -.
DR MaxQB; P25846; -.
DR PaxDb; P25846; -.
DR PRIDE; P25846; -.
DR EnsemblFungi; YHR120W_mRNA; YHR120W; YHR120W.
DR GeneID; 856520; -.
DR KEGG; sce:YHR120W; -.
DR SGD; S000001162; MSH1.
DR VEuPathDB; FungiDB:YHR120W; -.
DR eggNOG; ENOG502QUUG; Eukaryota.
DR HOGENOM; CLU_002472_4_0_1; -.
DR InParanoid; P25846; -.
DR OMA; MQCGDFY; -.
DR BioCyc; YEAST:G3O-31162-MON; -.
DR PRO; PR:P25846; -.
DR Proteomes; UP000002311; Chromosome VIII.
DR RNAct; P25846; protein.
DR GO; GO:0005739; C:mitochondrion; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008094; F:ATP-dependent activity, acting on DNA; IDA:SGD.
DR GO; GO:0140664; F:ATP-dependent DNA damage sensor activity; IEA:InterPro.
DR GO; GO:0032139; F:dinucleotide insertion or deletion binding; IDA:SGD.
DR GO; GO:0003690; F:double-stranded DNA binding; IBA:GO_Central.
DR GO; GO:0032137; F:guanine/thymine mispair binding; IDA:SGD.
DR GO; GO:0006281; P:DNA repair; IMP:SGD.
DR GO; GO:0006298; P:mismatch repair; IMP:SGD.
DR GO; GO:0043504; P:mitochondrial DNA repair; IMP:SGD.
DR GO; GO:0000002; P:mitochondrial genome maintenance; IMP:SGD.
DR GO; GO:0007005; P:mitochondrion organization; IMP:SGD.
DR Gene3D; 3.30.420.110; -; 1.
DR Gene3D; 3.40.1170.10; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR007695; DNA_mismatch_repair_MutS-lik_N.
DR InterPro; IPR017261; DNA_mismatch_repair_MutS/MSH.
DR InterPro; IPR000432; DNA_mismatch_repair_MutS_C.
DR InterPro; IPR007696; DNA_mismatch_repair_MutS_core.
DR InterPro; IPR016151; DNA_mismatch_repair_MutS_N.
DR InterPro; IPR036187; DNA_mismatch_repair_MutS_sf.
DR InterPro; IPR007860; DNA_mmatch_repair_MutS_con_dom.
DR InterPro; IPR036678; MutS_con_dom_sf.
DR InterPro; IPR045076; MutS_family.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR11361; PTHR11361; 1.
DR Pfam; PF01624; MutS_I; 1.
DR Pfam; PF05188; MutS_II; 1.
DR Pfam; PF05192; MutS_III; 1.
DR Pfam; PF00488; MutS_V; 1.
DR PIRSF; PIRSF037677; DNA_mis_repair_Msh6; 1.
DR SMART; SM00534; MUTSac; 1.
DR SMART; SM00533; MUTSd; 1.
DR SUPFAM; SSF48334; SSF48334; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF53150; SSF53150; 1.
DR SUPFAM; SSF55271; SSF55271; 1.
DR PROSITE; PS00486; DNA_MISMATCH_REPAIR_2; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Direct protein sequencing; DNA damage; DNA repair;
KW DNA-binding; Mitochondrion; Nucleotide-binding; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..21
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:7961998"
FT CHAIN 22..959
FT /note="DNA mismatch repair protein MSH1, mitochondrial"
FT /id="PRO_0000115179"
FT BINDING 771..778
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MUTAGEN 105
FT /note="F->A: Increases the rate of point mutations 35-fold
FT and displays a significant decrease in respiration-
FT competent cells during a time course."
FT /evidence="ECO:0000269|PubMed:15611870,
FT ECO:0000269|PubMed:16337661"
FT MUTAGEN 776
FT /note="G->D: Increases the rate of point mutations 19-fold
FT and displays a moderate decrease in respiration-competent
FT cells during a time course."
FT /evidence="ECO:0000269|PubMed:11862493,
FT ECO:0000269|PubMed:15611870, ECO:0000269|PubMed:16337661"
FT MUTAGEN 813
FT /note="R->W: Slightly increases the frequency of point
FT mutations and repeat-mediated deletion rates in mtDNA."
FT /evidence="ECO:0000269|PubMed:11862493,
FT ECO:0000269|PubMed:16337661"
FT CONFLICT 437
FT /note="T -> N (in Ref. 1; AAA34801)"
FT /evidence="ECO:0000305"
FT CONFLICT 695
FT /note="E -> V (in Ref. 1; AAA34801)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 959 AA; 109409 MW; F40985CB4D2ECFF1 CRC64;
MKHFFRLPTA FRPISRVSLR YSSTDTAQPK ISKLKISFNK ISESNSEKKD NLGSIDTRNC
LSTQQDDKLS STEPSKASLP PSLQYVRDLM DLYKDHVVLT QMGSFYELYF EQAIRYAPEL
NISLTNRAYS HGKVPFAGFP VHQLSRHLKM LVNNCGYSVT IAEQFKKKDV ADNEANKFYR
RVTRIVTPGT FIDEAFENLR ENTYLLNIEF PENCMSQVAD TSLKVGICWC DVSTGEIFVQ
QVYLRDLVSA ITRIQPKEIL LDERLLEFHI ESGTWYPELV ELKKFFIKYQ KMPSQHRTIE
SFYGLFNLGG KEATERQLKI QFQTFTQKEL AALRNTLIYV SNHLPDFSIN FQIPQRQLAT
AIMQIDSRTS TALELHSTVR DNNKKGSLLS SIRRTVTPSG TRLLSQWLSG PSLDLKEIKK
RQKIVAFFKD NRDITETLRT MLKKVNDLSR ILQKFSFGRG EALELIQMAR SLEVSREIRK
YLLNNTSLMK ATLKSQITQL TESLNFEKNL IDDILKFLNE EELAKSQDAK QNADVTRMLD
IDVKDKKESN KDEIFELRDF IVNPSFNTKL RKLHDTYQGV WQKKTEYNAL LKGFFVGDLG
AKTFTLKERQ NGEYALHVTG TASSLKKIDE LISKSTEYHG SCFHILQKSS QTRWLSHKIW
TDLGHELELL NLKIRNEEAN IIDLFKRKFI DRSNEVRQVA TTLGYLDTLS SFAVLANERN
LVCPKVDESN KLEVVNGRHL MVEEGLSARS LETFTANNCE LAKDNLWVIT GPNMGGKSTF
LRQNAIIVIL AQIGCFVPCS KARVGIVDKL FSRVGSADDL YNEMSTFMVE MIETSFILQG
ATERSLAILD EIGRGTSGKE GISIAYATLK YLLENNQCRT LFATHFGQEL KQIIDNKCSK
GMSEKVKFYQ SGITDLGGNN FCYNHKLKPG ICTKSDAIRV AELAGFPMEA LKEAREILG
