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Gene Review

PMS1  -  Pms1p

Saccharomyces cerevisiae S288c

Synonyms: DNA mismatch repair protein PMS1, N2317, Postmeiotic segregation protein 1, YNL082W
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Disease relevance of PMS1


High impact information on PMS1

  • We show here that mutations in any three yeast genes involved in DNA mismatch repair (PMS1, MLH1 and MSH2) lead to 100- to 700-fold increases in tract instability, whereas mutations that eliminate the proof-reading function of DNA polymerases have little effect [4].
  • We have studied the correction of heteroduplex plasmid DNA in pms1 mutant strains of Saccharomyces cerevisiae, which are known to exhibit higher frequencies of 5:3 type tetrads and lower frequencies of 6:2 tetrads than wild-type strains [5].
  • Our results suggest that the pms1 mutation causes a defect in mismatch correction, supporting the hypothesis that meiotic gene conversion in wild-type yeast cells often results from the correction of heteroduplex DNA [5].
  • MLH1, PMS1, and MSH2 interactions during the initiation of DNA mismatch repair in yeast [6].
  • A pol3-01/pol3-01 pms1/pms1 diploid was viable and displayed an estimated URA3 relative mutation rate of 2 x 10(4), which we calculate to be catastrophically high in a haploid [1].

Biological context of PMS1

  • Mutations in the yeast DNA mismatch repair genes MSH2, PMS1, and MLH1 increase the frequency of mutations for normal DNA sequences and destabilize microsatellites [7].
  • We examined the role of MSH2 and PMS1, yeast homologs of mutS and mutL, respectively, in the repair of base pair mismatches formed during meiotic recombination [8].
  • Both reduced and increased expression of PMS1 resulted in a mitotic mutator phenotype [9].
  • Regulation of the PMS1 gene was dependent on intact MluI cell cycle boxes, as demonstrated by analysis of a promoter mutant [9].
  • We found that all mutS homologues (MSH1-6) were induced during meiosis, whereas no evidence for regulation of the mutL homologues (PMS1, MLH1-3) was obtained [10].

Anatomical context of PMS1


Associations of PMS1 with chemical compounds

  • The MLH1-PMS1 heterodimer then interacts with the MSH proteins at or near the mismatch site and is thought to act as a mediator to recruit downstream repair proteins [12].
  • Additionally, the NH2 end coding region of PMS1 is found in the 3' end of the sequence [13].
  • Interestingly, double mutants in the MLH1 and PMS1 genes were deficient in TCR of thymine glycols [14].
  • Furthermore, two-hybrid analysis suggested that these ATP-binding-induced conformational changes promote an interaction between the NH(2) termini of Mlh1p and Pms1p [15].
  • Mlh1-Pms1 also binds to DNA, but independently of a mismatch [16].

Physical interactions of PMS1

  • Three approaches, ATP hydrolysis assays, limited proteolysis protection, and equilibrium dialysis, provide evidence that the amino-terminal domain of Mlh1 binds ATP with >10-fold higher affinity than does the amino-terminal domain of Pms1 [17].
  • We propose that the inhibition of conversion by large inserts is due to recognition by the Msh2/Pms1 complex of mismatches created by intrastrand interactions in the heteroduplex loop [18].

Regulatory relationships of PMS1

  • Overexpression of the PMS1 gene alone caused a moderate increase in the mutation rate and strongly suppressed the mutator effect caused by MLH1 overexpression [19].
  • The hsm3 mutation suppressed synthetic lethality in the hsm3 pol3-01 pms1 triple mutant and dramatically increased the spontaneous mutation rate in comparison with double mutant [20].
  • In contrast to their similar antimutator roles, Pms1p consistently inhibited recombination to a lesser degree than did Msh2p [21].

Other interactions of PMS1

  • Of these, MLH1 and PMS1 are known to act in the MSH2-dependent pathway that repairs DNA mismatches [22].
  • The mismatch repair mutations pms1, msh2 and msh3 did not affect 31- and 61-bp deletions in the pol3-t but increased the rates of 7- and 1-bp deletions [23].
  • In contrast to the pol3-t, the enhancement of 1-bp deletions in a rad52 mutant is not altered by a pms1 mutation [23].
  • Epistasis analysis of double mutants shows that the PMS1 and HSM3 genes control different mismatch repair systems [24].
  • Mismatch repair proteins Msh6, Pms1, and Mlh1 are not required [25].

Analytical, diagnostic and therapeutic context of PMS1


  1. Pathway correcting DNA replication errors in Saccharomyces cerevisiae. Morrison, A., Johnson, A.L., Johnston, L.H., Sugino, A. EMBO J. (1993) [Pubmed]
  2. Functional domains of the Saccharomyces cerevisiae Mlh1p and Pms1p DNA mismatch repair proteins and their relevance to human hereditary nonpolyposis colorectal cancer-associated mutations. Pang, Q., Prolla, T.A., Liskay, R.M. Mol. Cell. Biol. (1997) [Pubmed]
  3. Nucleotide sequence of the Salmonella typhimurium mutL gene required for mismatch repair: homology of MutL to HexB of Streptococcus pneumoniae and to PMS1 of the yeast Saccharomyces cerevisiae. Mankovich, J.A., McIntyre, C.A., Walker, G.C. J. Bacteriol. (1989) [Pubmed]
  4. Destabilization of tracts of simple repetitive DNA in yeast by mutations affecting DNA mismatch repair. Strand, M., Prolla, T.A., Liskay, R.M., Petes, T.D. Nature (1993) [Pubmed]
  5. The role of heteroduplex correction in gene conversion in Saccharomyces cerevisiae. Bishop, D.K., Williamson, M.S., Fogel, S., Kolodner, R.D. Nature (1987) [Pubmed]
  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 (1994) [Pubmed]
  7. Mutations in the MSH3 gene preferentially lead to deletions within tracts of simple repetitive DNA in Saccharomyces cerevisiae. Strand, M., Earley, M.C., Crouse, G.F., Petes, T.D. Proc. Natl. Acad. Sci. U.S.A. (1995) [Pubmed]
  8. Interaction between mismatch repair and genetic recombination in Saccharomyces cerevisiae. Alani, E., Reenan, R.A., Kolodner, R.D. Genetics (1994) [Pubmed]
  9. Transcription of mutS and mutL-homologous genes in Saccharomyces cerevisiae during the cell cycle. Kramer, W., Fartmann, B., Ringbeck, E.C. Mol. Gen. Genet. (1996) [Pubmed]
  10. Transcription of mutS- and mutL-homologous genes during meiosis in Saccharomyces cerevisiae and identification of a regulatory cis-element for meiotic induction of MSH2. Meyer, C., Scheller, J., Kramer, W. Mol. Genet. Genomics (2001) [Pubmed]
  11. Analysis of yeast pms1, msh2, and mlh1 mutators points to differences in mismatch correction efficiencies between prokaryotic and eukaryotic cells. Yang, Y., Karthikeyan, R., Mack, S.E., Vonarx, E.J., Kunz, B.A. Mol. Gen. Genet. (1999) [Pubmed]
  12. Msh2 separation of function mutations confer defects in the initiation steps of mismatch repair. Kijas, A.W., Studamire, B., Alani, E. J. Mol. Biol. (2003) [Pubmed]
  13. The sequence of a 17,933 bp segment of Saccharomyces cerevisiae chromosome XIV contains the RHO2, TOP2, MKT1 and END3 genes and five new open reading frames. Soler-Mira, A., Saiz, J.E., Ballesta, J.P., Remacha, M. Yeast (1996) [Pubmed]
  14. Requirement for DNA mismatch repair proteins in the transcription-coupled repair of thymine glycols in Saccharomyces cerevisiae. Leadon, S.A., Avrutskaya, A.V. Mutat. Res. (1998) [Pubmed]
  15. Functional studies on the candidate ATPase domains of Saccharomyces cerevisiae MutLalpha. Tran, P.T., Liskay, R.M. Mol. Cell. Biol. (2000) [Pubmed]
  16. DNA binding properties of the yeast Msh2-Msh6 and Mlh1-Pms1 heterodimers. Drotschmann, K., Hall, M.C., Shcherbakova, P.V., Wang, H., Erie, D.A., Brownewell, F.R., Kool, E.T., Kunkel, T.A. Biol. Chem. (2002) [Pubmed]
  17. Differential ATP binding and intrinsic ATP hydrolysis by amino-terminal domains of the yeast Mlh1 and Pms1 proteins. Hall, M.C., Shcherbakova, P.V., Kunkel, T.A. J. Biol. Chem. (2002) [Pubmed]
  18. (CA/TG) microsatellite sequences escape the inhibition of recombination by mismatch repair in Saccharomyces cerevisiae. Gendrel, C.G., Dutreix, M. Genetics (2001) [Pubmed]
  19. Inactivation of DNA mismatch repair by increased expression of yeast MLH1. Shcherbakova, P.V., Hall, M.C., Lewis, M.S., Bennett, S.E., Martin, K.J., Bushel, P.R., Afshari, C.A., Kunkel, T.A. Mol. Cell. Biol. (2001) [Pubmed]
  20. Requirement of HSM3 gene for spontaneous mutagenesis in Saccharomyces cerevisiae. Fedorova, I.V., Kovaltzova, S.V., Gracheva, L.M., Evstuhina, T.A., Korolev, V.G. Mutat. Res. (2004) [Pubmed]
  21. Regulation of mitotic homeologous recombination in yeast. Functions of mismatch repair and nucleotide excision repair genes. Nicholson, A., Hendrix, M., Jinks-Robertson, S., Crouse, G.F. Genetics (2000) [Pubmed]
  22. 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. (1998) [Pubmed]
  23. The prevention of repeat-associated deletions in Saccharomyces cerevisiae by mismatch repair depends on size and origin of deletions. Tran, H.T., Gordenin, D.A., Resnick, M.A. Genetics (1996) [Pubmed]
  24. The yeast HSM3 gene acts in one of the mismatch repair pathways. Fedorova, I.V., Gracheva, L.M., Kovaltzova, S.V., Evstuhina, T.A., Alekseev, S.Y., Korolev, V.G. Genetics (1998) [Pubmed]
  25. Role of Saccharomyces cerevisiae Msh2 and Msh3 repair proteins in double-strand break-induced recombination. Sugawara, N., Pâques, F., Colaiácovo, M., Haber, J.E. Proc. Natl. Acad. Sci. U.S.A. (1997) [Pubmed]
  26. Analysis of interactions between mismatch repair initiation factors and the replication processivity factor PCNA. Lee, S.D., Alani, E. J. Mol. Biol. (2006) [Pubmed]
  27. High affinity cooperative DNA binding by the yeast Mlh1-Pms1 heterodimer. Hall, M.C., Wang, H., Erie, D.A., Kunkel, T.A. J. Mol. Biol. (2001) [Pubmed]
  28. Mutagenesis of yeast MW104-1B strain has identified the uncharacterized PMS6 DNA mismatch repair gene locus and additional alleles of existing PMS1, PMS2 and MSH2 genes. Jeyaprakash, A., Welch, J.W., Fogel, S. Mutat. Res. (1994) [Pubmed]
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