Linked Life Data

10924150

Source:http://linkedlifedata.com/resource/pubmed/id/10924150

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
31
pubmed:dateCreated
2000-9-7
pubmed:abstractText
S100 proteins are small dimeric members of the EF-hand superfamily of Ca(2+) binding proteins thought to participate in mediating intracellular Ca(2+) signals by binding to and thereby regulating target proteins in a Ca(2+)-dependent manner. As dimer formation is crucial to S100 function, we applied a yeast two-hybrid approach in analyzing in vivo molecular aspects of S100 dimerization. We chose S100P, a member of the S100 family highly expressed in placenta, for detailed analysis and showed that S100P monomers strongly interact with one another but not with other S100 polypeptides, indicating that homodimer formation is obligatory for S100P. Analysis of the interaction of site-specific S100P mutants with the wild-type polypeptide or with other S100P mutant chains identifies conserved hydrophobic amino acid residues involved in mediating dimerization in vivo. Of these residues, F-15 is crucially important as a mutation to alanine abolishes dimerization even when the F15A S100P mutant polypeptide is allowed to interact with a wild-type chain. On the other hand, I-11, I-12, or F-89 need to be replaced by a less hydrophopic residue in both subunits for there to be a similar extent of interfere with dimerization. This proves that hydrophobic residues implicated through structural studies in S100 dimerization are involved in the dimer interaction in vivo and argues for a hierarchy of hydrophobic contacts stabilizing the dimer and thereby regulating S100 function.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0006-2960
pubmed:author
pubmed:issnType
Print
pubmed:day
8
pubmed:volume
39
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
9533-9
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:10924150-Amino Acid Sequence, pubmed-meshheading:10924150-Amino Acids, pubmed-meshheading:10924150-Blotting, Western, pubmed-meshheading:10924150-Calcium-Binding Proteins, pubmed-meshheading:10924150-Cloning, Molecular, pubmed-meshheading:10924150-DNA, Complementary, pubmed-meshheading:10924150-Dimerization, pubmed-meshheading:10924150-Humans, pubmed-meshheading:10924150-Molecular Sequence Data, pubmed-meshheading:10924150-Mutagenesis, Site-Directed, pubmed-meshheading:10924150-Neoplasm Proteins, pubmed-meshheading:10924150-Peptide Fragments, pubmed-meshheading:10924150-Plasmids, pubmed-meshheading:10924150-Protein Structure, Secondary, pubmed-meshheading:10924150-Saccharomyces cerevisiae, pubmed-meshheading:10924150-Transformation, Genetic, pubmed-meshheading:10924150-Two-Hybrid System Techniques
pubmed:year
2000
pubmed:articleTitle
Identification of hydrophobic amino acid residues involved in the formation of S100P homodimers in vivo.
pubmed:affiliation
Institute for Medical Biochemistry, University of Münster, Germany.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't