Linked Life Data

12826664

Source:http://linkedlifedata.com/resource/pubmed/id/12826664

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
36
pubmed:dateCreated
2003-9-1
pubmed:abstractText
Association of the highly conserved heterochromatin protein, HP1, with the specialized chromatin of centromeres and telomeres requires binding to a specific histone H3 modification of methylation on lysine 9. This modification is catalyzed by the Drosophila Su(var)3-9 gene product and its homologues. Specific DNA binding activities are also likely to be required for targeting this activity along with HP1 to specific chromosomal regions. The Drosophila HOAP protein is a DNA-binding protein that was identified as a component of a multiprotein complex of HP1 containing Drosophila origin recognition complex (ORC) subunits in the early Drosophila embryo. Here we show direct physical interactions between the HOAP protein and HP1 and specific ORC subunits. Two additional HP1-like proteins (HP1b and HP1c) were recently identified in Drosophila, and the unique chromosomal distribution of each isoform is determined by two independently acting HP1 domains (hinge and chromoshadow domain) (47). We find heterochromatin protein 1/origin recognition complex-associated protein (HOAP) to interact specifically with the originally described predominantly heterochromatic HP1a protein. Both the hinge and chromoshadow domains of HP1a are required for its interaction with HOAP, and a novel peptide repeat located in the carboxyl terminus of the HOAP protein is required for the interaction with the HP1 hinge domain. Peptides that interfere with HP1a/HOAP interactions in co-precipitation experiments also displace HP1 from the heterochromatic chromocenter of polytene chromosomes in larval salivary glands. A mutant for the HOAP protein also suppresses centric heterochromatin-induced silencing, supporting a role for HOAP in centric heterochromatin.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
5
pubmed:volume
278
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
34491-8
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed-meshheading:12826664-Amino Acid Motifs, pubmed-meshheading:12826664-Amino Acid Sequence, pubmed-meshheading:12826664-Animals, pubmed-meshheading:12826664-Chromatin, pubmed-meshheading:12826664-Chromatography, Gel, pubmed-meshheading:12826664-Chromosomal Proteins, Non-Histone, pubmed-meshheading:12826664-Chromosomes, pubmed-meshheading:12826664-Crosses, Genetic, pubmed-meshheading:12826664-DNA-Binding Proteins, pubmed-meshheading:12826664-Drosophila, pubmed-meshheading:12826664-Drosophila Proteins, pubmed-meshheading:12826664-Female, pubmed-meshheading:12826664-Heterochromatin, pubmed-meshheading:12826664-Immunoblotting, pubmed-meshheading:12826664-Male, pubmed-meshheading:12826664-Microscopy, Fluorescence, pubmed-meshheading:12826664-Molecular Sequence Data, pubmed-meshheading:12826664-Origin Recognition Complex, pubmed-meshheading:12826664-Peptides, pubmed-meshheading:12826664-Precipitin Tests, pubmed-meshheading:12826664-Protein Binding, pubmed-meshheading:12826664-Protein Structure, Tertiary, pubmed-meshheading:12826664-Recombinant Proteins, pubmed-meshheading:12826664-Telomere
pubmed:year
2003
pubmed:articleTitle
Novel Drosophila heterochromatin protein 1 (HP1)/origin recognition complex-associated protein (HOAP) repeat motif in HP1/HOAP interactions and chromocenter associations.
pubmed:affiliation
Department of Biology, University of Kentucky, Lexington, Kentucky 40506-0225, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.