PMID:9701520
| Citation |
Gabig, M, Obuchowski, M, Ciesielska, A, Latała, B, Wegrzyn, A, Thomas, MS and Wegrzyn, G (1998) The Escherichia coli RNA polymerase alpha subunit and transcriptional activation by bacteriophage lambda CII protein. Acta Biochim. Pol. 45:271-80 |
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| Abstract |
Bacteriophage lambda is not able to lysogenise the Escherichia coli rpoA341 mutant. This mutation causes a single amino acid substitution Lys271Glu in the C-terminal domain of the RNA polymerase alpha subunit (alphaCTD). Our previous studies indicated that the impaired lysogenisation of the rpoA341 host is due to a defect in transcriptional activation by the phage CII protein and suggested a role for alphaCTD in this process. Here we used a series of truncation and point mutants in the rpoA gene placed on a plasmid to investigate the process of transcriptional activation by the cII gene product. Our results indicate that amino-acid residues 265, 268 and 271 in the a subunit may play an important role in the CII-mediated activation of the pE promoter (most probably residue 271) or may be involved in putative interactions between alphaCTD and an UP-like element near pE (most probably residues 265 and 268). Measurement of the activity of pE-lacZ, pI-lacZ and p(aQ)-lacZ fusions in the rpoA+ and rpoA341 hosts demonstrated that the mechanism of activation of these CII-dependent promoters may be in each case different. |
| Links | |
| Keywords |
Artificial Gene Fusion; Bacteriophage lambda/genetics; DNA-Directed RNA Polymerases/genetics; Escherichia coli/enzymology; Escherichia coli/genetics; Genes, Bacterial; Lac Operon; Lysogeny; Peptide Fragments/genetics; Point Mutation; Promoter Regions, Genetic; Transcription Factors/genetics; Transcription, Genetic; Viral Proteins |
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