Identification of a subunit assembly domain in the alpha subunit of Escherichia coli RNA polymerase

1991 ◽  
Vol 218 (1) ◽  
pp. 1-6 ◽  
Author(s):  
Kazuhiko Igarashi ◽  
Nobuyuki Fujita ◽  
Akira Ishihama
Keyword(s):  
Escherichia Coli ◽  
Rna Polymerase ◽  
Alpha Subunit ◽  
Subunit Assembly ◽  
A Subunit

scholarly journals The Escherichia coli RNA polymerase alpha subunit and transcriptional activation by bacteriophage lambda CII protein.

1998 ◽  
Vol 45 (1) ◽  
pp. 271-280 ◽  
Author(s):  
M Gabig ◽  
M Obuchowski ◽  
A Ciesielska ◽  
B Latała ◽  
A Wegrzyn ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Amino Acid ◽  
Rna Polymerase ◽  
Transcriptional Activation ◽  
Bacteriophage Lambda ◽  
Alpha Subunit ◽  
Single Amino Acid ◽  
Amino Acid Residues ◽  
A Subunit ◽  
Rpoa Gene

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.

scholarly journals Intrasubunit nucleotide binding in ribonucleic acid polymerase

1978 ◽  
Vol 175 (1) ◽  
pp. 189-192 ◽  
Author(s):  
A D B Malcolm ◽  
J R Moffatt
Keyword(s):  
Escherichia Coli ◽  
Rna Polymerase ◽  
Ribonucleic Acid ◽  
Periodate Oxidation ◽  
Nucleotide Binding ◽  
Alpha Subunit ◽  
Nucleoside Triphosphate ◽  
Competitive Inhibitors ◽  
Nucleoside Triphosphates ◽  
Derivatives Of

1. Periodate oxidation of the ribose ring was used to synthesize derivatives of nucleoside triphosphates. 2. These oxidized nucleoside triphosphates. 2. These oxidized nucleoside triphosphates are competitive inhibitors of RNA polymerase. 3. On incubation, together with NaBH4, these oxidized labelled nucleotides are covalently bound to Escherichia coli RNA polymerase. 4. Nucleoside triphosphate substrates decrease the extent of labelling. 5. A lysine residue in an alpha-subunit is labelled. 6. The significance of these results in relation to the location of the nucleotide-binding site is discussed.

Functional Map of the Alpha Subunit of Escherichia coli RNA Polymerase

1994 ◽  
Vol 242 (2) ◽  
pp. 107-115 ◽  
Author(s):  
Makoto Kimura ◽  
Nobuyuki Fujita ◽  
Akira Ishihama
Keyword(s):  
Escherichia Coli ◽  
Rna Polymerase ◽  
Alpha Subunit ◽  
Functional Map
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