scholarly journals The rpoE gene encoding the sigma E (sigma 24) heat shock sigma factor of Escherichia coli.

1995 ◽  
Vol 14 (5) ◽  
pp. 1043-1055 ◽  
Author(s):  
S. Raina ◽  
D. Missiakas ◽  
C. Georgopoulos
1995 ◽  
Vol 14 (5) ◽  
pp. 1032-1042 ◽  
Author(s):  
P.E. Rouvière ◽  
A. De Las Peñas ◽  
J. Mecsas ◽  
C.Z. Lu ◽  
K.E. Rudd ◽  
...  

2000 ◽  
Vol 182 (2) ◽  
pp. 518-521 ◽  
Author(s):  
Christopher A. Conlin ◽  
Charles G. Miller

ABSTRACT The opdA (prlC) gene of Salmonella enterica serovar Typhimurium and Escherichia coliencodes the metalloprotease oligopeptidase A (OpdA). We report thatopdA is cotranscribed with a downstream open reading frame,yhiQ. Transcription of this operon is induced after a temperature shift (30 to 42°C), and this induction depends on the heat shock sigma factor encoded by the rpoH(htpR) gene.


1988 ◽  
Vol 170 (8) ◽  
pp. 3640-3649 ◽  
Author(s):  
Y N Zhou ◽  
N Kusukawa ◽  
J W Erickson ◽  
C A Gross ◽  
T Yura

2007 ◽  
Vol 189 (23) ◽  
pp. 8430-8436 ◽  
Author(s):  
Olga V. Kourennaia ◽  
Pieter L. deHaseth

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.


1997 ◽  
Vol 94 (20) ◽  
pp. 10967-10972 ◽  
Author(s):  
C.-H. Yeh ◽  
P.-F. L. Chang ◽  
K.-W. Yeh ◽  
W.-C. Lin ◽  
Y.-M. Chen ◽  
...  

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