scholarly journals Rickettsia prowazekii sigma factor  73 can be overexpressed in Escherichia coli and promotes RNA polymerase binding and transcription

Microbiology ◽  
1996 ◽  
Vol 142 (4) ◽  
pp. 901-906 ◽  
Author(s):  
L. P. Aniskovitch ◽  
H. H. Winkler
Keyword(s):  
Escherichia Coli ◽  
Rna Polymerase ◽  
Sigma Factor ◽  
Rickettsia Prowazekii ◽  
Polymerase Binding

scholarly journals Substitution of a Highly Conserved Histidine in the Escherichia coli Heat Shock Transcription Factor, σ32, Affects Promoter Utilization In Vitro and Leads to Overexpression of the Biofilm-Associated Flu Protein In Vivo

2007 ◽  
Vol 189 (23) ◽  
pp. 8430-8436 ◽  
Author(s):  
Olga V. Kourennaia ◽  
Pieter L. deHaseth
Keyword(s):  
Escherichia Coli ◽  
Heat Shock ◽  
Rna Polymerase ◽  
Sigma Factor ◽  
Stable Complex ◽  
Tryptophan Residue ◽  
Specific Sequence ◽  
Bacterial Rna

ABSTRACT The heat shock sigma factor (σ32 in Escherichia coli) directs the bacterial RNA polymerase to promoters of a specific sequence to form a stable complex, competent to initiate transcription of genes whose products mitigate the effects of exposure of the cell to high temperatures. The histidine at position 107 of σ32 is at the homologous position of a tryptophan residue at position 433 of the main sigma factor of E. coli, σ70. This tryptophan is essential for the strand separation step leading to the formation of the initiation-competent RNA polymerase-promoter complex. The heat shock sigma factors of all gammaproteobacteria sequenced have a histidine at this position, while in the alpha- and deltaproteobacteria, it is a tryptophan. In vitro the alanine-for-histidine substitution at position 107 (H107A) destabilizes complexes between the GroE promoter and RNA polymerase containing σ32, implying that H107 plays a role in formation or maintenance of the strand-separated complex. In vivo, the H107A substitution in σ32 impedes recovery from heat shock (exposure to 42°C), and it also leads to overexpression at lower temperatures (30°C) of the Flu protein, which is associated with biofilm formation.

scholarly journals Structure-function comparisons of (p)ppApp vs (p)ppGpp for Escherichia coli RNA polymerase binding sites and for rrnB P1 promoter regulatory responses in vitro

2018 ◽  
Vol 1861 (8) ◽  
pp. 731-742 ◽  
Author(s):  
Bożena Bruhn-Olszewska ◽  
Vadim Molodtsov ◽  
Michał Sobala ◽  
Maciej Dylewski ◽  
Katsuhiko S. Murakami ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Rna Polymerase ◽  
Structure Function ◽  
Binding Sites ◽  
Polymerase Binding

scholarly journals A novel RNA polymerase‐binding protein that interacts with a sigma‐factor docking site

2017 ◽  
Vol 105 (4) ◽  
pp. 652-662 ◽  
Author(s):  
Anna F. Wang Erickson ◽  
Padraig Deighan ◽  
Shanshan Chen ◽  
Kelsey Barrasso ◽  
Cinthia P. Garcia ◽  
...  
Keyword(s):  
Rna Polymerase ◽  
Sigma Factor ◽  
Binding Protein ◽  
Docking Site ◽  
Polymerase Binding
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