| pubmed-article:7933095 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:7933095 | lifeskim:mentions | umls-concept:C1335858 | lld:lifeskim |
| pubmed-article:7933095 | lifeskim:mentions | umls-concept:C0029005 | lld:lifeskim |
| pubmed-article:7933095 | lifeskim:mentions | umls-concept:C1704675 | lld:lifeskim |
| pubmed-article:7933095 | lifeskim:mentions | umls-concept:C2755756 | lld:lifeskim |
| pubmed-article:7933095 | pubmed:issue | 11 | lld:pubmed |
| pubmed-article:7933095 | pubmed:dateCreated | 1994-11-17 | lld:pubmed |
| pubmed-article:7933095 | pubmed:abstractText | We previously showed that v-Rel, the oncoprotein of the avian retrovirus Rev-T, can increase expression from promoters containing binding sites for the cellular transcription factor Sp1 in chicken embryo fibroblasts (S. Sif, A.J. Capobianco, and T.D. Gilmore, Oncogene 8:2501-2509, 1993). In those experiments, v-Rel appeared to increase the transactivating function of Sp1; that is, v-Rel stimulated transactivation by a GAL4-Sp1 protein that lacked the Sp1 DNA-binding domain. We have now shown that in vitro-synthesized v-Rel and GAL4-Sp1 form a complex that can be immunoprecipitated with either anti-Sp1 or anti-v-Rel antiserum. We have also shown that a glutathione S-transferase (GST)-Sp1 fusion protein can specifically interact with in vitro-translated v-Rel and with in vivo-synthesized v-Rel from transformed chicken spleen cells. In addition, we have found that the abilities of wild-type and two mutant forms of v-Rel to increase transactivation by Sp1 in vivo correlate with their abilities to interact with Sp1 in vitro. The sequences important for the interaction of v-Rel with Sp1 in vitro have been mapped to the first 147 amino acids of v-Rel. Other Rel proteins, such as c-Rel, RelA, p52, and p50, were also able to form a complex with Sp1 in vitro. These results suggest that v-Rel increases expression from Sp1 site-containing promoters by functionally interacting with Sp1 and that cellular Rel proteins and Sp1 are likely to interact to influence transcription from natural promoters. | lld:pubmed |
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| pubmed-article:7933095 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:7933095 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:7933095 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:7933095 | pubmed:month | Nov | lld:pubmed |
| pubmed-article:7933095 | pubmed:issn | 0022-538X | lld:pubmed |
| pubmed-article:7933095 | pubmed:author | pubmed-author:SimTT | lld:pubmed |
| pubmed-article:7933095 | pubmed:author | pubmed-author:GilmoreT DTD | lld:pubmed |
| pubmed-article:7933095 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:7933095 | pubmed:volume | 68 | lld:pubmed |
| pubmed-article:7933095 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:7933095 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:7933095 | pubmed:pagination | 7131-8 | lld:pubmed |
| pubmed-article:7933095 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:7933095 | pubmed:meshHeading | pubmed-meshheading:7933095-... | lld:pubmed |
| pubmed-article:7933095 | pubmed:year | 1994 | lld:pubmed |
| pubmed-article:7933095 | pubmed:articleTitle | Interaction of the v-Rel oncoprotein with cellular transcription factor Sp1. | lld:pubmed |
| pubmed-article:7933095 | pubmed:affiliation | Department of Biology, Boston University, Massachusetts 02215. | lld:pubmed |
| pubmed-article:7933095 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:7933095 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:7933095 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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