| pubmed-article:9499408 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:9499408 | lifeskim:mentions | umls-concept:C0014834 | lld:lifeskim |
| pubmed-article:9499408 | lifeskim:mentions | umls-concept:C0035681 | lld:lifeskim |
| pubmed-article:9499408 | lifeskim:mentions | umls-concept:C1336776 | lld:lifeskim |
| pubmed-article:9499408 | lifeskim:mentions | umls-concept:C0439836 | lld:lifeskim |
| pubmed-article:9499408 | lifeskim:mentions | umls-concept:C1879547 | lld:lifeskim |
| pubmed-article:9499408 | lifeskim:mentions | umls-concept:C1521840 | lld:lifeskim |
| pubmed-article:9499408 | lifeskim:mentions | umls-concept:C1711351 | lld:lifeskim |
| pubmed-article:9499408 | pubmed:issue | 5 | lld:pubmed |
| pubmed-article:9499408 | pubmed:dateCreated | 1998-4-9 | lld:pubmed |
| pubmed-article:9499408 | pubmed:abstractText | Evidence obtained in both eukaryotes and prokaryotes indicates that arbitrary contacts between DNA-bound proteins and components of the transcriptional machinery can activate transcription. Here we demonstrate that the Escherichia coli omega protein, which copurifies with RNA polymerase, can function as a transcriptional activator when linked covalently to a DNA-binding protein. We show further that omega can function as an activation target when this covalent linkage is replaced by a pair of interacting polypeptides fused to the DNA-binding protein and to omega, respectively. Our findings imply that the omega protein is associated with RNA polymerase holoenzyme in vivo, and provide support for the hypothesis that contact between a DNA-bound protein and any component of E. coli RNA polymerase can activate transcription. | lld:pubmed |
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| pubmed-article:9499408 | pubmed:language | eng | lld:pubmed |
| pubmed-article:9499408 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9499408 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:9499408 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:9499408 | pubmed:month | Mar | lld:pubmed |
| pubmed-article:9499408 | pubmed:issn | 0890-9369 | lld:pubmed |
| pubmed-article:9499408 | pubmed:author | pubmed-author:DoveS LSL | lld:pubmed |
| pubmed-article:9499408 | pubmed:author | pubmed-author:HochschildAA | lld:pubmed |
| pubmed-article:9499408 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:9499408 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:9499408 | pubmed:volume | 12 | lld:pubmed |
| pubmed-article:9499408 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:9499408 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:9499408 | pubmed:pagination | 745-54 | lld:pubmed |
| pubmed-article:9499408 | pubmed:dateRevised | 2010-9-13 | lld:pubmed |
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| pubmed-article:9499408 | pubmed:meshHeading | pubmed-meshheading:9499408-... | lld:pubmed |
| pubmed-article:9499408 | pubmed:year | 1998 | lld:pubmed |
| pubmed-article:9499408 | pubmed:articleTitle | Conversion of the omega subunit of Escherichia coli RNA polymerase into a transcriptional activator or an activation target. | lld:pubmed |
| pubmed-article:9499408 | pubmed:affiliation | Department of Microbiology and Molecular Genetics, Harvard Medical School, Boston, Massachusetts 02115, USA. | lld:pubmed |
