Linked Life Data

10777662

Source:http://linkedlifedata.com/resource/pubmed/id/10777662

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
2000-6-5
pubmed:databankReference
pubmed:abstractText
Schizosaccharomyces pombe hus1 promotes radioresistance and hydroxyurea resistance, as well as S and G2 phase checkpoint control. We isolated a human cDNA homologous to hus1, called HUS1. The major focus of this report is on a detailed analysis of the physical interactions of the HUS1-encoded protein and two other checkpoint control proteins, RAD1p and RAD9p, implicated in the cellular response to DNA damage. We found that HUS1p interacts with itself and the N-terminal region of RAD1p. In contrast, the C-terminal portion of the checkpoint protein RAD9p is essential for interacting with HUS1p and the C-terminal region of RAD1p. Since the N-terminal portion of RAD9p was previously demonstrated to participate in apoptosis, this protein likely has at least two functional domains, one that regulates programmed cell death and another that regulates cell cycle checkpoint control. Truncated versions of HUS1p are unable to bind RAD1p, RAD9p, or another HUS1p molecule. RAD1p-RAD1p and RAD9p-RAD9p interactions can be demonstrated by coimmunoprecipitation, but not by two-hybrid analysis, suggesting that the proteins associate as part of a complex but do not interact directly. Northern blot analysis indicates that HUS1 is expressed in different tissues, but the mRNA is most predominant in testis where high levels of RAD1 and RAD9 message have been detected. These studies suggest that HUS1p, RAD9p, and RAD1p form a complex in human cells and may function in a meiotic checkpoint in addition to the cell cycle delays induced by incomplete DNA replication or DNA damage.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0888-7543
pubmed:author
pubmed:copyrightInfo
Copyright 2000 Academic Press.
pubmed:issnType
Print
pubmed:day
1
pubmed:volume
65
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
24-33
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed-meshheading:10777662-Binding Sites, pubmed-meshheading:10777662-Blotting, Northern, pubmed-meshheading:10777662-Cell Cycle, pubmed-meshheading:10777662-Cell Cycle Proteins, pubmed-meshheading:10777662-DNA, Complementary, pubmed-meshheading:10777662-DNA, Recombinant, pubmed-meshheading:10777662-Exonucleases, pubmed-meshheading:10777662-Female, pubmed-meshheading:10777662-Gene Expression Regulation, pubmed-meshheading:10777662-Humans, pubmed-meshheading:10777662-Macromolecular Substances, pubmed-meshheading:10777662-Male, pubmed-meshheading:10777662-Molecular Sequence Data, pubmed-meshheading:10777662-Precipitin Tests, pubmed-meshheading:10777662-Protein Binding, pubmed-meshheading:10777662-RNA, Messenger, pubmed-meshheading:10777662-Schizosaccharomyces pombe Proteins, pubmed-meshheading:10777662-Sequence Analysis, DNA, pubmed-meshheading:10777662-Tissue Distribution, pubmed-meshheading:10777662-Two-Hybrid System Techniques
pubmed:year
2000
pubmed:articleTitle
Physical interactions among human checkpoint control proteins HUS1p, RAD1p, and RAD9p, and implications for the regulation of cell cycle progression.
pubmed:affiliation
Center for Radiological Research, Columbia University, 630 West 168th Street, New York, NY, 10032, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, U.S. Gov't, Non-P.H.S.