Mutation to rifampicin resistance at the beginning of the RNA polymerase β subunit gene in Escherichia coli

1984 ◽  
Vol 196 (1) ◽  
pp. 173-174 ◽  
Author(s):  
N. A. Lisitsyn ◽  
E. D. Sverdlov ◽  
E. P. Moiseyeva ◽  
O. N. Danilevskaya ◽  
V. G. Nikiforov
1981 ◽  
Vol 184 (3) ◽  
pp. 536-538 ◽  
Author(s):  
Yu. A. Ovchinnikov ◽  
G. S. Monastyrskaya ◽  
V. V. Gubanov ◽  
V. M. Lipkin ◽  
E. D. Sverdlov ◽  
...  

2010 ◽  
Vol 192 (21) ◽  
pp. 5580-5587 ◽  
Author(s):  
Tamara D. James ◽  
Michael Cashel ◽  
Deborah M. Hinton

ABSTRACT During infection of Escherichia coli, bacteriophage T4 usurps the host transcriptional machinery, redirecting it to the expression of early, middle, and late phage genes. Middle genes, whose expression begins about 1 min postinfection, are transcribed both from the extension of early RNA into middle genes and by the activation of T4 middle promoters. Middle-promoter activation requires the T4 transcriptional activator MotA and coactivator AsiA, which are known to interact with σ70, the specificity subunit of RNA polymerase. T4 motA amber [motA(Am)] or asiA(Am) phage grows poorly in wild-type E. coli. However, previous work has found that T4 motA(Am)does not grow in the E. coli mutant strain TabG. We show here that the RNA polymerase in TabG contains two mutations within its β-subunit gene: rpoB(E835K) and rpoB(G1249D). We find that the G1249D mutation is responsible for restricting the growth of either T4 motA(Am)or asiA(Am) and for impairing transcription from MotA/AsiA-activated middle promoters in vivo. With one exception, transcription from tested T4 early promoters is either unaffected or, in some cases, even increases, and there is no significant growth phenotype for the rpoB(E835K G1249D) strain in the absence of T4 infection. In reported structures of thermophilic RNA polymerase, the G1249 residue is located immediately adjacent to a hydrophobic pocket, called the switch 3 loop. This loop is thought to aid in the separation of the RNA from the DNA-RNA hybrid as RNA enters the RNA exit channel. Our results suggest that the presence of MotA and AsiA may impair the function of this loop or that this portion of the β subunit may influence interactions among MotA, AsiA, and RNA polymerase.


Gene ◽  
1980 ◽  
Vol 11 (3-4) ◽  
pp. 367-373 ◽  
Author(s):  
Geneviève Delcuve ◽  
Willa Downing ◽  
Hilary Lewis ◽  
Patrick P. Dennis

1981 ◽  
Vol 183 (1) ◽  
pp. 54-58 ◽  
Author(s):  
Ben A. Oostra ◽  
Klaas Kok ◽  
Adri J. Van Vliet ◽  
AB Geert ◽  
Max Gruber

2017 ◽  
Vol 27 (6) ◽  
pp. 356-362 ◽  
Author(s):  
Eugene Y. Wu ◽  
Angela K. Hilliker

Rifampicin is an effective antibiotic against mycobacterial and other bacterial infections, but resistance readily emerges in laboratory and clinical settings. We screened <i>Escherichia coli</i> for rifampicin resistance and identified numerous mutations to the gene encoding the β-chain of RNA polymerase (<i>rpoB</i>), including an unusual 9-nucleotide deletion mutation. Structural modeling of the deletion mutant indicates locations of potential steric clashes with rifampicin. Sequence conservation in the region near the deletion mutation suggests a similar mutation may also confer resistance during the treatment of tuberculosis.


DNA Repair ◽  
2007 ◽  
Vol 6 (10) ◽  
pp. 1434-1440 ◽  
Author(s):  
Ann K. Ganesan ◽  
Abigail J. Smith ◽  
Nigel J. Savery ◽  
Portia Zamos ◽  
Philip C. Hanawalt

1986 ◽  
Vol 203 (2) ◽  
pp. 265-268 ◽  
Author(s):  
Robert E. Glass ◽  
Steven T. Jones ◽  
Akira Ishihama

1982 ◽  
Vol 188 (3) ◽  
pp. 399-404 ◽  
Author(s):  
Vishvanath Nene ◽  
Robert E. Glass

2011 ◽  
Vol 80 (5) ◽  
pp. 1169-1185 ◽  
Author(s):  
Ganduri Swapna ◽  
Atanu Chakraborty ◽  
Vandana Kumari ◽  
Ranjan Sen ◽  
Valakunja Nagaraja

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