PMS1 ATP-binding mismatch repair protein [Saccharomyces cerevisiae S288C] - Gene

Summary

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Official Symbol: PMS1
Official Full Name: ATP-binding mismatch repair protein
Primary source: SGD:S000005026
Locus tag: YNL082W
See related: AllianceGenome:SGD:S000005026; FungiDB:YNL082W; VEuPathDB:YNL082W
Gene type: protein coding
RefSeq status: REVIEWED
Organism: Saccharomyces cerevisiae S288C (strain: S288C)
Lineage: Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces
Summary: Enables ATP binding activity and ATP hydrolysis activity. Contributes to dinucleotide insertion or deletion binding activity; heteroduplex DNA loop binding activity; and single-stranded DNA binding activity. Involved in meiotic mismatch repair. Located in cytoplasm and nucleus. Part of MutLalpha complex. Human ortholog(s) of this gene implicated in Lynch syndrome; hereditary nonpolyposis colorectal cancer type 4; mismatch repair cancer syndrome; ovarian cancer; and urinary bladder cancer. Orthologous to several human genes including PMS2 (PMS1 homolog 2, mismatch repair system component). [provided by Alliance of Genome Resources, Dec 2024]
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Genomic context

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See PMS1 in Genome Data Viewer

Location:: chromosome: XIV

Exon count:: 1

Sequence:: Chromosome: XIV; NC_001146.8 (473391..476012)

Chromosome XIV - NC_001146.8 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:: NC_001146.8

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

Experimental exchange of paralogous domains in the MLH family provides evidence of sub-functionalization after gene duplication.
Title: Experimental exchange of paralogous domains in the MLH family provides evidence of sub-functionalization after gene duplication.
Handcuffing intrinsically disordered regions in Mlh1-Pms1 disrupts mismatch repair.
Title: Handcuffing intrinsically disordered regions in Mlh1-Pms1 disrupts mismatch repair.
Results provide evidence that the PMS1 gene encoding one of the crucial components of the mismatch repair, is required for transcriptional repression at silent mating-type loci and telomeres.
Title: Yeast mismatch repair components are required for stable inheritance of gene silencing.
Mlh1-Pms1 complexes with shorter IDRs that disrupt MMR retain wild-type DNA binding affinity but are impaired for diffusion on both naked and nucleosome-coated DNA. Moreover, the IDRs also regulate the adenosine triphosphate hydrolysis and nuclease activities that are encoded in the structured N- and C-terminal domains of the complex
Title: Intrinsically disordered regions regulate both catalytic and non-catalytic activities of the MutLα mismatch repair complex.
Genotyping analysis indicated that MLH1-PMS1 incompatibility was the major driver of mutation rate in the isolates. The variation in the mutation rate of incompatible spore clones could be due to background suppressors and enhancers, as well as aneuploidy seen in the spore clones.
Title: Incompatibilities in Mismatch Repair Genes MLH1-PMS1 Contribute to a Wide Range of Mutation Rates in Human Isolates of Baker's Yeast.
Two mutants of MutLalpha, pms1-G882E and pms1-H888R, repair deletion mispairs but not insertion mispairs.
Title: Different roles of eukaryotic MutS and MutL complexes in repair of small insertion and deletion loops in yeast.
a comparative study of Msh2-Msh3 and Msh2-Msh6 for mispair binding, sliding clamp formation, and Mlh1-Pms1 recruitment
Title: Mispair-specific recruitment of the Mlh1-Pms1 complex identifies repair substrates of the Saccharomyces cerevisiae Msh2-Msh3 complex.
The unstructured linker arms of Mlh1-Pms1 are important for interactions with DNA during mismatch repair
Title: The unstructured linker arms of Mlh1-Pms1 are important for interactions with DNA during mismatch repair.
Functional residues on the surface of the N-terminal domain of yeast Pms1
Title: Functional residues on the surface of the N-terminal domain of yeast Pms1.
Adenine nucleotides induce large asymmetric conformational changes in full-length yeast MutL alpha. These changes are associated with significant increases in secondary structure.
Title: Direct visualization of asymmetric adenine-nucleotide-induced conformational changes in MutL alpha.

Submit: New GeneRIF Correction See all GeneRIFs (13)

Pathways from PubChem

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Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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Homology

Orthologs from OrthoDB

Gene Ontology Provided by SGD

Function	Evidence Code	Pubs
enables ATP binding	IEA Inferred from Electronic Annotation more info
enables ATP binding	IMP Inferred from Mutant Phenotype more info	PubMed
enables ATP hydrolysis activity	IBA Inferred from Biological aspect of Ancestor more info
enables ATP hydrolysis activity	IDA Inferred from Direct Assay more info	PubMed
enables ATP hydrolysis activity	IEA Inferred from Electronic Annotation more info
enables ATP hydrolysis activity	IMP Inferred from Mutant Phenotype more info	PubMed
enables ATP-dependent DNA damage sensor activity	IEA Inferred from Electronic Annotation more info
contributes_to DNA insertion or deletion binding	IDA Inferred from Direct Assay more info	PubMed
contributes_to dinucleotide insertion or deletion binding	IDA Inferred from Direct Assay more info	PubMed
contributes_to double-stranded DNA binding	IDA Inferred from Direct Assay more info	PubMed
contributes_to heteroduplex DNA loop binding	IDA Inferred from Direct Assay more info	PubMed
enables mismatched DNA binding	IEA Inferred from Electronic Annotation more info
contributes_to single-stranded DNA binding	IDA Inferred from Direct Assay more info	PubMed
enables zinc ion binding	RCA inferred from Reviewed Computational Analysis more info	PubMed

Process	Evidence Code	Pubs
involved_in DNA repair	IEA Inferred from Electronic Annotation more info
involved_in meiosis I cell cycle process	IEA Inferred from Electronic Annotation more info
involved_in meiotic mismatch repair	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in mismatch repair	IBA Inferred from Biological aspect of Ancestor more info
involved_in mismatch repair	IEA Inferred from Electronic Annotation more info
involved_in mismatch repair	IMP Inferred from Mutant Phenotype more info	PubMed

Component	Evidence Code	Pubs
part_of MutLalpha complex	IBA Inferred from Biological aspect of Ancestor more info
part_of MutLalpha complex	IPI Inferred from Physical Interaction more info	PubMed
located_in cytoplasm	HDA more info	PubMed
part_of mismatch repair complex	IEA Inferred from Electronic Annotation more info
located_in nucleus	HDA more info	PubMed
located_in nucleus	IEA Inferred from Electronic Annotation more info

General protein information

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Preferred Names: ATP-binding mismatch repair protein

NP_014317.4

ATP-binding protein required for mismatch repair; required for both mitosis and meiosis; functions as a heterodimer with Mlh1p; binds double- and single-stranded DNA via its N-terminal domain; required for silencing at the silent mating-type loci and telomeres; similar to E. coli MutL

NCBI Reference Sequences (RefSeq)

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Genome Annotation

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference assembly

Genomic

NC_001146.8 Reference assembly

Range

473391..476012

Download

GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

NM_001182920.3 → NP_014317.4 TPA: ATP-binding mismatch repair protein [Saccharomyces cerevisiae S288C]

See identical proteins and their annotated locations for NP_014317.4

Status: REVIEWED

UniProtKB/Swiss-Prot

D6W197, P14242, Q2I044, Q2I045, Q45TY4, Q8TG48, Q8TG50, Q8TG54, Q8TG57

UniProtKB/TrEMBL

A6ZRZ8, B3LNU1, C8ZGE8, N1P4G0

Conserved Domains (1) summary

COG0323
Location:1 → 870

MutL; DNA mismatch repair ATPase MutL [Replication, recombination and repair]