Linked Life Data

11112423

Source:http://linkedlifedata.com/resource/pubmed/id/11112423

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
2000-12-26
pubmed:abstractText
We cloned cDNA encoding the chicken p46 polypeptide, chp46, homologous to the p48 subunit of chicken chromatin assembly factor-1, chCAF-1p48. It comprises 424 amino acids including a putative initiation Met, is a member of the WD protein family, with seven WD repeat motifs, and exhibits 90.3% identity to chCAF-1p48 and 94.3% identity to the human and mouse p46 polypeptides (hup46 and mop46). The in vitro immunoprecipitation experiment established that chp46 interacts with histones H2B and H4 and chicken histone acetyltransferase-1, chHAT-1, whereas hup46 interacts with histones H2A and H4 and chHAT-1 and chCAF-1p48 with histone H4 and chHAT-1. The in vitro immunoprecipitation experiment, involving truncated mutants of chp46, revealed not only that two regions comprising amino acids 33-179 and 375-404 are necessary for its binding to H2B, but also that two regions comprising amino acids 1-32 and 405-424 are necessary for its binding to H4. Furthermore, the GST pulldown affinity assay, involving truncated mutants of chp46, revealed that a region comprising amino acids 359-404 (in fact, 375-404) binds to chHAT-1 in vitro. Taken together, these results indicate not only that chp46 should participate differentially in a number of DNA-utilizing processes through interactions of its distinct regions with chHAT-1 and histones H2B and H4, but also that the proper propeller structure of chp46 is not necessary for its interaction with chHAT-1.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0006-291X
pubmed:author
pubmed:copyrightInfo
Copyright 2000 Academic Press.
pubmed:issnType
Print
pubmed:day
9
pubmed:volume
279
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
95-102
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed-meshheading:11112423-Acetyltransferases, pubmed-meshheading:11112423-Amino Acid Sequence, pubmed-meshheading:11112423-Animals, pubmed-meshheading:11112423-Base Sequence, pubmed-meshheading:11112423-Chickens, pubmed-meshheading:11112423-Chromatin Assembly Factor-1, pubmed-meshheading:11112423-Chromosomal Proteins, Non-Histone, pubmed-meshheading:11112423-Cloning, Molecular, pubmed-meshheading:11112423-DNA, Complementary, pubmed-meshheading:11112423-DNA Primers, pubmed-meshheading:11112423-DNA-Binding Proteins, pubmed-meshheading:11112423-Histone Acetyltransferases, pubmed-meshheading:11112423-Histones, pubmed-meshheading:11112423-Molecular Sequence Data, pubmed-meshheading:11112423-Protein Binding, pubmed-meshheading:11112423-Saccharomyces cerevisiae Proteins, pubmed-meshheading:11112423-Sequence Homology, Amino Acid
pubmed:year
2000
pubmed:articleTitle
Distinct regions of the chicken p46 polypeptide are required for its in vitro interaction with histones H2B and H4 and histone acetyltransferase-1.
pubmed:affiliation
Department of Biochemistry, Miyazaki Medical College, 5200, Kihara, Kiyotake, Miyazaki 889-1692, Japan.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't