PMS1/YNL082W Summary Help

Standard Name PMS1 1
Systematic Name YNL082W
Feature Type ORF, Verified
Description ATP-binding protein required for mismatch repair in mitosis and meiosis; functions as a heterodimer with Mlh1p, binds double- and single-stranded DNA via its N-terminal domain, similar to E. coli MutL (1, 2, 3 and see Summary Paragraph)
Name Description PostMeiotic Segregation 1
Chromosomal Location
ChrXIV:473391 to 476012 | ORF Map | GBrowse
Gbrowse
Genetic position: -66 cM
Gene Ontology Annotations All PMS1 GO evidence and references
  View Computational GO annotations for PMS1
Molecular Function
Manually curated
Biological Process
Manually curated
Cellular Component
Manually curated
High-throughput
Mutant phenotypes All PMS1 Phenotype evidence and references
Classical genetics
null
reduction of function
unspecified
Large-scale survey
null
Resources
interactions All PMS1 Interaction evidence and references
99 total interaction(s) for 47 unique genes/features.
Physical Interactions
  • Affinity Capture-MS: 8
  • Affinity Capture-Western: 2
  • Co-crystal Structure: 1
  • Co-purification: 3
  • Reconstituted Complex: 6
  • Two-hybrid: 12
Genetic Interactions
  • Dosage Growth Defect: 2
  • Dosage Lethality: 1
  • Dosage Rescue: 1
  • Negative Genetic: 17
  • Phenotypic Enhancement: 31
  • Phenotypic Suppression: 1
  • Positive Genetic: 4
  • Synthetic Growth Defect: 4
  • Synthetic Lethality: 6
Resources
Expression Summary
histogram
Resources
Protein Information All PMS1 Protein evidence and references
Localization
Phosphorylation PhosphoGRID | PhosphoPep Database
Structure
Homologs
sequence information
ChrXIV:473391 to 476012 | ORF Map | GBrowse
SGD ORF map
Genetic position: -66 cM
Last Update Coordinates: 2011-02-03 | Sequence: 2004-04-21
Subfeature details
Relative
Coordinates		 Chromosomal
Coordinates		 Most Recent Updates
Coordinates Sequence
CDS 1..2622 473391..476012 2011-02-03 2004-04-21
Retrieve sequences
Analyze Sequence
S288C only
S288C vs. other species
S288C vs. other strains
Resources
External Links All Associated Seq | Entrez Gene | Entrez RefSeq Protein | MIPS | Search all NCBI (Entrez) | UniProtKB
Primary SGDIDS000005026
SUMMARY PARAGRAPH for PMS1

PMS1, one of four MutL homologs in S. cerevisiae, is involved in mismatch repair during mitosis and meiosis (reviewed in 4, 5). Pms1p is involved in the repair of mismatches caused by errors during replication (6) as well as the repair of DNA damage caused by cisplatin, alkylating agents, and oxidation (7). Pms1p is also involved in the correction of mismatches that arise during the formation of heteroduplex DNA between two homologous chromosomes during meiotic recombination (8). Failure to repair these mismatches during meiosis leads to an increase of post-meiotic segregation (PMS) events in which the 4:4 Mendelian segregation pattern of the 8 single-strands of DNA is altered to a 5:3 non-Mendelian segregation pattern. Consistent with its multiple roles in mismatch repair, a pms1 mutant displays a severe mutator phenotype as well as an increase in PMS events (1, 9, 6, 10).

Pms1p forms a heterodimer with Mlh1p, one of the other MutL homologs in S. cerevisiae (11, 12, 10). The Mlh1p-Pms1p heterodimer plays a major role in mismatch repair but a limited role in meiotic crossing-over. Although the Mlh1p-Pms1p heterodimer does not bind mismatched DNA, it interacts with both Msh2p-Msh3p and Msh2-Msh6p heterodimers during mismatch repair (13, 14, 15, 16).

The S. cerevisiae PMS1 is related to the human hPMS2 (OMIM)(17), which forms a heterodimer with hMLH1 (18 and references within). Because S. cerevisiae Pms1p and Mlh1p from different strain backgrounds display a mutator phenotype when combined, variations in hPMS2 and hMLH1 may lead to hereditary nonpolyposis colorectal cancer (HNPCC)-like (OMIM) cancers with atypical inheritance patterns (19 and references within).

Last updated: 2007-05-29

References cited on this page View Complete Literature Guide for PMS1
1) Williamson MS, et al.  (1985) Meiotic gene conversion mutants in Saccharomyces cerevisiae. I. Isolation and characterization of pms1-1 and pms1-2. Genetics 110(4):609-46
2) Hall MC, et al.  (2002) Differential ATP binding and intrinsic ATP hydrolysis by amino-terminal domains of the yeast Mlh1 and Pms1 proteins. J Biol Chem 277(5):3673-9
3) Hall MC, et al.  (2003) DNA binding by yeast Mlh1 and Pms1: implications for DNA mismatch repair. Nucleic Acids Res 31(8):2025-34
4) Kolodner RD and Marsischky GT  (1999) Eukaryotic DNA mismatch repair. Curr Opin Genet Dev 9(1):89-96
5) Borts RH, et al.  (2000) The many faces of mismatch repair in meiosis. Mutat Res 451(1-2):129-50
6) Strand M, et al.  (1993) Destabilization of tracts of simple repetitive DNA in yeast by mutations affecting DNA mismatch repair. Nature 365(6443):274-6
7) Simon JA, et al.  (2000) Differential toxicities of anticancer agents among DNA repair and checkpoint mutants of Saccharomyces cerevisiae. Cancer Res 60(2):328-33
8) Bishop DK, et al.  (1987) The role of heteroduplex correction in gene conversion in Saccharomyces cerevisiae. Nature 328(6128):362-4
9) Prolla TA, et al.  (1994) Dual requirement in yeast DNA mismatch repair for MLH1 and PMS1, two homologs of the bacterial mutL gene. Mol Cell Biol 14(1):407-15
10) Wang TF, et al.  (1999) Functional specificity of MutL homologs in yeast: evidence for three Mlh1-based heterocomplexes with distinct roles during meiosis in recombination and mismatch correction. Proc Natl Acad Sci U S A 96(24):13914-9
11) Prolla TA, et al.  (1994) MLH1, PMS1, and MSH2 interactions during the initiation of DNA mismatch repair in yeast. Science 265(5175):1091-3
12) Pang Q, et al.  (1997) Functional domains of the Saccharomyces cerevisiae Mlh1p and Pms1p DNA mismatch repair proteins and their relevance to human hereditary nonpolyposis colorectal cancer-associated mutations. Mol Cell Biol 17(8):4465-73
13) Habraken Y, et al.  (1997) Enhancement of MSH2-MSH3-mediated mismatch recognition by the yeast MLH1-PMS1 complex. Curr Biol 7(10):790-3
14) Habraken Y, et al.  (1998) ATP-dependent assembly of a ternary complex consisting of a DNA mismatch and the yeast MSH2-MSH6 and MLH1-PMS1 protein complexes. J Biol Chem 273(16):9837-41
15) Mendillo ML, et al.  (2005) Analysis of the interaction between the Saccharomyces cerevisiae MSH2-MSH6 and MLH1-PMS1 complexes with DNA using a reversible DNA end-blocking system. J Biol Chem 280(23):22245-57
16) Stone JE and Petes TD  (2006) 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. Genetics 173(3):1223-39
17) Horii A, et al.  (1994) Cloning, characterization and chromosomal assignment of the human genes homologous to yeast PMS1, a member of mismatch repair genes. Biochem Biophys Res Commun 204(3):1257-64
18) Kolodner RD  (1995) Mismatch repair: mechanisms and relationship to cancer susceptibility. Trends Biochem Sci 20(10):397-401
19) Heck JA, et al.  (2006) Negative epistasis between natural variants of the Saccharomyces cerevisiae MLH1 and PMS1 genes results in a defect in mismatch repair. Proc Natl Acad Sci U S A 103(9):3256-61