Linked Life Data

10092617

Source:http://linkedlifedata.com/resource/pubmed/id/10092617

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
14
pubmed:dateCreated
1999-4-27
pubmed:abstractText
Distinct biochemical activities have been reported for small and large molecular complexes of heat shock protein 27 (HSP27), respectively. Using glycerol gradient ultracentrifugation and chemical cross-linking, we show here that Chinese hamster HSP27 is expressed in cells as homotypic multimers ranging from dimers up to 700-kDa oligomers. Treatments with arsenite, which induces phosphorylation on Ser15 and Ser90, provoked a major change in the size distribution of the complexes that shifted from oligomers to dimers. Ser90 phosphorylation was sufficient and necessary for causing this change in structure. Dimer formation was severely inhibited by replacing Ser90 with Ala90 but not by replacing Ser15 with Ala15. Using the yeast two-hybrid system, two domains were identified that were responsible for HSP27 intermolecular interactions. One domain was insensitive to phosphorylation and corresponded to the C-terminal alpha-crystallin domain. The other domain was sensitive to serine 90 phosphorylation and was located in the N-terminal region of the protein. Fusion of this N-terminal domain to firefly luciferase conferred luciferase with the capacity to form multimers that dissociated into monomers upon phosphorylation. A deletion within this domain of residues Arg5-Tyr23, which contains a WDPF motif found in most proteins of the small heat shock protein family, yielded a protein that forms only phosphorylation-insensitive dimers. We propose that HSP27 forms stable dimers through the alpha-crystallin domain. These dimers further multimerize through intermolecular interactions mediated by the phosphorylation-sensitive N-terminal domain.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
2
pubmed:volume
274
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
9378-85
pubmed:dateRevised
2007-11-15
pubmed:meshHeading
pubmed-meshheading:10092617-3T3 Cells, pubmed-meshheading:10092617-Amino Acid Sequence, pubmed-meshheading:10092617-Animals, pubmed-meshheading:10092617-Beetles, pubmed-meshheading:10092617-CHO Cells, pubmed-meshheading:10092617-Conserved Sequence, pubmed-meshheading:10092617-Cricetinae, pubmed-meshheading:10092617-Dimerization, pubmed-meshheading:10092617-Heat-Shock Proteins, pubmed-meshheading:10092617-Intracellular Signaling Peptides and Proteins, pubmed-meshheading:10092617-Luciferases, pubmed-meshheading:10092617-Mice, pubmed-meshheading:10092617-Molecular Sequence Data, pubmed-meshheading:10092617-Molecular Weight, pubmed-meshheading:10092617-Neoplasm Proteins, pubmed-meshheading:10092617-Phosphorylation, pubmed-meshheading:10092617-Protein-Serine-Threonine Kinases, pubmed-meshheading:10092617-Serine, pubmed-meshheading:10092617-Structure-Activity Relationship, pubmed-meshheading:10092617-Transfection, pubmed-meshheading:10092617-Ultracentrifugation
pubmed:year
1999
pubmed:articleTitle
HSP27 multimerization mediated by phosphorylation-sensitive intermolecular interactions at the amino terminus.
pubmed:affiliation
Centre de recherche en cancérologie de l'Université Laval, L'Hôtel-Dieu de Québec, Québec, Québec G1R 2J6, Canada.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't