| pubmed-article:8120097 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8120097 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:8120097 | lifeskim:mentions | umls-concept:C0041197 | lld:lifeskim |
| pubmed-article:8120097 | lifeskim:mentions | umls-concept:C0006732 | lld:lifeskim |
| pubmed-article:8120097 | lifeskim:mentions | umls-concept:C1419786 | lld:lifeskim |
| pubmed-article:8120097 | lifeskim:mentions | umls-concept:C1167622 | lld:lifeskim |
| pubmed-article:8120097 | pubmed:issue | 5 | lld:pubmed |
| pubmed-article:8120097 | pubmed:dateCreated | 1994-4-4 | lld:pubmed |
| pubmed-article:8120097 | pubmed:abstractText | The cDNA coding for mouse fibroblast tropomyosin isoform 2 (TM2) was placed into a bacterial expression vector to produce a fusion protein containing glutathione-S-transferase (GST) and TM2 (GST/TM2). Glutathione-Sepharose beads bearing GST/TM2 were incubated with [35S]methionine-labeled NIH 3T3 cell extracts and the materials bound to the fusion proteins were analyzed to identify proteins that interact with TM2. A protein of 10 kD was found to bind to GST/TM2, but not to GST. The binding of the 10-kD protein to GST/TM2 was dependent on the presence of Ca2+ and inhibited by molar excess of free TM2 in a competition assay. The 10-kD protein-binding site was mapped to the region spanning residues 39-107 on TM2 by using several COOH-terminal and NH2-terminal truncation mutants of TM2. The 10-kD protein was isolated from an extract of NIH 3T3 cells transformed by v-Ha-ras by affinity chromatography on a GST/TM2 truncation mutant followed by SDS-PAGE and electroelution. Partial amino acid sequence analysis of the purified 10-kD protein, two-dimensional polyacrylamide gel analysis and a binding experiment revealed that the 10-kD protein was identical to a calcium-binding protein derived from mRNA named pEL98 or 18A2 that is homologous to S100 protein. Immunoblot analysis of the distribution of the 10-kD protein in Triton-soluble and -insoluble fractions of NIH 3T3 cells revealed that some of the 10-kD protein was associated with the Triton-insoluble cytoskeletal residue in a Ca(2+)-dependent manner. Furthermore, immunofluorescent staining of NIH 3T3 cells showed that some of the 10-kD protein colocalized with nonmuscle TMs in microfilament bundles. These results suggest that some of the pEL98 protein interacts with microfilament-associated nonmuscle TMs in NIH 3T3 cells. | lld:pubmed |
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| pubmed-article:8120097 | pubmed:language | eng | lld:pubmed |
| pubmed-article:8120097 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8120097 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:8120097 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:8120097 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8120097 | pubmed:month | Mar | lld:pubmed |
| pubmed-article:8120097 | pubmed:issn | 0021-9525 | lld:pubmed |
| pubmed-article:8120097 | pubmed:author | pubmed-author:SatoKK | lld:pubmed |
| pubmed-article:8120097 | pubmed:author | pubmed-author:HasegawaYY | lld:pubmed |
| pubmed-article:8120097 | pubmed:author | pubmed-author:EndoHH | lld:pubmed |
| pubmed-article:8120097 | pubmed:author | pubmed-author:NakamuraYY | lld:pubmed |
| pubmed-article:8120097 | pubmed:author | pubmed-author:TakenagaKK | lld:pubmed |
| pubmed-article:8120097 | pubmed:author | pubmed-author:SakiyamaSS | lld:pubmed |
| pubmed-article:8120097 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8120097 | pubmed:volume | 124 | lld:pubmed |
| pubmed-article:8120097 | pubmed:geneSymbol | v-Ha-ras | lld:pubmed |
| pubmed-article:8120097 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8120097 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8120097 | pubmed:pagination | 757-68 | lld:pubmed |
| pubmed-article:8120097 | pubmed:dateRevised | 2010-10-6 | lld:pubmed |
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