Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
1999-8-5
pubmed:databankReference
pubmed:abstractText
The human PMS2 gene encodes one of the bacterial mutL homologs that is associated with hereditary nonpolyposis colorectal cancer (HNPCC). One of the interesting features of the hPMS2 gene is that it is part of a multiple gene family which is localized on chromosome bands 7p22, 7p12-p13, 7q11, and 7q22. Here we report four newly identified hPMS2-like (PMS2L) genes. All four novel members of the PMS2L gene family encode relatively short polypeptides composed of the amino-terminal portion of hPMS2 and are expressed ubiquitously except in the heart. To clarify whether the PMS2L polypeptides contribute to the DNA mismatch repair (MMR) pathway through an interaction with hMLH1, we have performed a yeast two-hybrid assay and an immunoprecipitation study using an hPMS2 mutant cell line, HEC-1-A. Our results clearly indicate that hMLH1 does not interact with two representative PMS2Ls, whereas the carboxyl-terminal portion of hPMS2, not the amino-terminal portion, does interact with hMLH1. Thus, PMS2Ls are not likely to participate in the MMR pathway through association with hMLH1; they must play some other roles in the living cells.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Adaptor Proteins, Signal Transducing, http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Triphosphatases, http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins, http://linkedlifedata.com/resource/pubmed/chemical/DNA, Complementary, http://linkedlifedata.com/resource/pubmed/chemical/DNA Repair Enzymes, http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins, http://linkedlifedata.com/resource/pubmed/chemical/MLH1 protein, human, http://linkedlifedata.com/resource/pubmed/chemical/Neoplasm Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Proteins, http://linkedlifedata.com/resource/pubmed/chemical/PMS2 protein, human, http://linkedlifedata.com/resource/pubmed/chemical/Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0021-924X
pubmed:author
pubmed:issnType
Print
pubmed:volume
125
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
818-25
pubmed:dateRevised
2007-12-19
pubmed:meshHeading
pubmed-meshheading:10101297-Adaptor Proteins, Signal Transducing, pubmed-meshheading:10101297-Adenosine Triphosphatases, pubmed-meshheading:10101297-Amino Acid Sequence, pubmed-meshheading:10101297-Base Pair Mismatch, pubmed-meshheading:10101297-Base Sequence, pubmed-meshheading:10101297-Carrier Proteins, pubmed-meshheading:10101297-Cell Line, pubmed-meshheading:10101297-DNA, Complementary, pubmed-meshheading:10101297-DNA Repair, pubmed-meshheading:10101297-DNA Repair Enzymes, pubmed-meshheading:10101297-DNA-Binding Proteins, pubmed-meshheading:10101297-Gene Expression, pubmed-meshheading:10101297-Humans, pubmed-meshheading:10101297-Molecular Sequence Data, pubmed-meshheading:10101297-Multigene Family, pubmed-meshheading:10101297-Neoplasm Proteins, pubmed-meshheading:10101297-Nuclear Proteins, pubmed-meshheading:10101297-Proteins, pubmed-meshheading:10101297-Recombinant Proteins, pubmed-meshheading:10101297-Saccharomyces cerevisiae, pubmed-meshheading:10101297-Sequence Homology, Amino Acid
pubmed:year
1999
pubmed:articleTitle
The human PMS2L proteins do not interact with hMLH1, a major DNA mismatch repair protein.
pubmed:affiliation
Department of Molecular Pathology, Tohoku University School of Medicine, Sendai, Miyagi, 980-8575, Japan.
pubmed:publicationType
Journal Article, In Vitro, Research Support, Non-U.S. Gov't