Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
2003-12-3
pubmed:abstractText
We previously reported not only that chicken HIRA, a homolog of Saccharomyces cerevisiae transcriptional corepressors Hir1p and Hir2p, possesses seven WD dipeptide motifs and a LXXLL motif in its N-terminal half and C-terminal half, respectively, but also that the N-terminal and C-terminal halves, respectively, bind to CAF-1p48 and HDAC-1 and -2 in vitro. Seven WD dipeptide motifs in the N-terminal half of HIRA are required for the in vitro interaction with CAF-1p48. The LXXLL motif at positions 993-997 of HIRA is necessary for the in vitro interaction with HDAC-2. Here we revealed not only that the N-terminal and C-terminal halves of HIRA mediate individually transcription repressions but also that even one of the seven WD dipeptide motifs and the LXXLL motif of HIRA are essential for the mediations in vivo. Moreover, the LXXLL motif is essential for the interaction with endogenous or recombinant HDAC-2 in vivo, probably resulting in formation of the active complex, harboring the HDAC activity. Taken together, these results indicate that HIRA should participate differentially in a number of DNA-utilizing processes, including transcription repressions, through interactions of its distinct regions with CAF-1p48 and HDAC-2, respectively.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0006-291X
pubmed:author
pubmed:issnType
Print
pubmed:day
26
pubmed:volume
312
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1266-72
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed-meshheading:14652010-Amino Acid Motifs, pubmed-meshheading:14652010-Animals, pubmed-meshheading:14652010-Binding Sites, pubmed-meshheading:14652010-COS Cells, pubmed-meshheading:14652010-Cell Cycle Proteins, pubmed-meshheading:14652010-Cercopithecus aethiops, pubmed-meshheading:14652010-Chickens, pubmed-meshheading:14652010-Dipeptides, pubmed-meshheading:14652010-HeLa Cells, pubmed-meshheading:14652010-Histone Chaperones, pubmed-meshheading:14652010-Histone Deacetylase 2, pubmed-meshheading:14652010-Histone Deacetylases, pubmed-meshheading:14652010-Humans, pubmed-meshheading:14652010-Nuclear Proteins, pubmed-meshheading:14652010-Protein Binding, pubmed-meshheading:14652010-Repressor Proteins, pubmed-meshheading:14652010-Structure-Activity Relationship, pubmed-meshheading:14652010-Transcription, Genetic, pubmed-meshheading:14652010-Transcription Factors
pubmed:year
2003
pubmed:articleTitle
WD dipeptide motifs and LXXLL motif of chicken HIRA are necessary for transcription repression and the latter motif is essential for interaction with histone deacetylase-2 in vivo.
pubmed:affiliation
Department of Life Science, Frontier Science Research Center, University of Miyazaki, 5200, Kihara, Kiyotake, 889-1692, Miyazaki, Japan.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't