| pubmed-article:1740119 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:1740119 | lifeskim:mentions | umls-concept:C0229671 | lld:lifeskim |
| pubmed-article:1740119 | lifeskim:mentions | umls-concept:C0205145 | lld:lifeskim |
| pubmed-article:1740119 | lifeskim:mentions | umls-concept:C0031715 | lld:lifeskim |
| pubmed-article:1740119 | lifeskim:mentions | umls-concept:C0108555 | lld:lifeskim |
| pubmed-article:1740119 | lifeskim:mentions | umls-concept:C1704632 | lld:lifeskim |
| pubmed-article:1740119 | lifeskim:mentions | umls-concept:C0871261 | lld:lifeskim |
| pubmed-article:1740119 | lifeskim:mentions | umls-concept:C0442805 | lld:lifeskim |
| pubmed-article:1740119 | lifeskim:mentions | umls-concept:C2911692 | lld:lifeskim |
| pubmed-article:1740119 | lifeskim:mentions | umls-concept:C1706817 | lld:lifeskim |
| pubmed-article:1740119 | lifeskim:mentions | umls-concept:C1521828 | lld:lifeskim |
| pubmed-article:1740119 | lifeskim:mentions | umls-concept:C0678640 | lld:lifeskim |
| pubmed-article:1740119 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:1740119 | pubmed:dateCreated | 1992-3-25 | lld:pubmed |
| pubmed-article:1740119 | pubmed:abstractText | Recombinant baculoviruses were used to express wild-type serum response factor (SRF) and a mutant, SRF.CKIIA, which lacks all four serine residues in the major casein kinase II (CKII) site at residues 77-90. Purified recombinant SRF binds DNA with an affinity and specificity indistinguishable from that of HeLa cell SRF, and activates transcription in vitro. Comparative phosphopeptide analysis of the wild-type and mutant proteins demonstrated that the wild-type protein is phosphorylated at the major CKII site in insect cells. Dephosphorylation of recombinant SRF does not affect its affinity for the c-fos SRE, and results in only a 3-fold reduction in binding to the synthetic site ACT.L. However, dephosphorylation does cause a large decrease in the rates of association with and dissociation from either site. These effects are due solely to phosphorylation at the major CKII site: the binding properties of the SRF.CKIIA mutant are identical to those of dephosphorylated wild-type SRF, and CKII phosphorylation in vitro converts dephosphorylated wild-type SRF from a slow-binding to a fast-binding form without significantly changing binding affinity. CKII phosphorylation thus acts to potentiate SRF-DNA exchange rates rather than alter equilibrium binding affinity. | lld:pubmed |
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| pubmed-article:1740119 | pubmed:language | eng | lld:pubmed |
| pubmed-article:1740119 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1740119 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:1740119 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:1740119 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:1740119 | pubmed:month | Jan | lld:pubmed |
| pubmed-article:1740119 | pubmed:issn | 0261-4189 | lld:pubmed |
| pubmed-article:1740119 | pubmed:author | pubmed-author:WynneJJ | lld:pubmed |
| pubmed-article:1740119 | pubmed:author | pubmed-author:TreismanRR | lld:pubmed |
| pubmed-article:1740119 | pubmed:author | pubmed-author:HsuanJ JJJ | lld:pubmed |
| pubmed-article:1740119 | pubmed:author | pubmed-author:McGuiganCC | lld:pubmed |
| pubmed-article:1740119 | pubmed:author | pubmed-author:MaraisR MRM | lld:pubmed |
| pubmed-article:1740119 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:1740119 | pubmed:volume | 11 | lld:pubmed |
| pubmed-article:1740119 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:1740119 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:1740119 | pubmed:pagination | 97-105 | lld:pubmed |
| pubmed-article:1740119 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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