Phenotypic analysis of Salmonella enterica serovar Typhimurium rpoE mutants encoding RNA polymerase extracytoplasmic stress response sigma factors σE with altered promoter specificity

2012 ◽  
Vol 195 (1) ◽  
pp. 27-36 ◽  
Author(s):  
Bronislava Rezuchova ◽  
Dagmar Homerova ◽  
Beatrica Sevcikova ◽  
Renata Novakova ◽  
Lubomira Feckova ◽  
...  
Microbiology ◽  
2007 ◽  
Vol 153 (1) ◽  
pp. 263-269 ◽  
Author(s):  
Alisdair McMeechan ◽  
Mark Roberts ◽  
Tristan A. Cogan ◽  
Frieda Jørgensen ◽  
Andrew Stevenson ◽  
...  

2006 ◽  
Vol 188 (22) ◽  
pp. 7988-7991 ◽  
Author(s):  
Grace Yim ◽  
Fernando de la Cruz ◽  
George B. Spiegelman ◽  
Julian Davies

ABSTRACT Promoter-lux fusions that showed rifampin-modulated transcription were identified from a Salmonella enterica serovar Typhimurium 14028 reporter library. The transformation of a subset of fusions into mutants that lacked one of six global regulatory proteins or were rifampin resistant showed that transcription modulation was independent of the global regulators, promoter specific, and dependent on the interaction of rifampin with RNA polymerase.


Microbiology ◽  
2007 ◽  
Vol 153 (7) ◽  
pp. 2148-2158 ◽  
Author(s):  
William J Kenyon ◽  
Kristy L Nicholson ◽  
Bronislava Rezuchova ◽  
Dagmar Homerova ◽  
Francisco Garcia-del Portillo ◽  
...  

2006 ◽  
Vol 188 (18) ◽  
pp. 6703-6708 ◽  
Author(s):  
Shouji Yamamoto ◽  
Kazuhiro Kutsukake

ABSTRACT Flagellar operons are divided into three classes with respect to their transcriptional hierarchy in Salmonella enterica serovar Typhimurium. The class 1 gene products FlhD and FlhC act together in an FlhD2C2 heterotetramer, which binds upstream of the class 2 promoters to facilitate binding of RNA polymerase. Class 2 expression is known to be enhanced by a disruption mutation in a flagellar gene, fliT. In this study, we purified FliT protein in a His-tagged form and showed that the protein prevented binding of FlhD2C2 to the class 2 promoter and inhibited FlhD2C2-dependent transcription. Pull-down and far-Western blotting analyses revealed that the FliT protein was capable of binding to FlhD2C2 and FlhC and not to FlhD alone. We conclude that FliT acts as an anti-FlhD2C2 factor, which binds to FlhD2C2 through interaction with the FlhC subunit and inhibits its binding to the class 2 promoter.


RNA Biology ◽  
2016 ◽  
Vol 13 (3) ◽  
pp. 331-342 ◽  
Author(s):  
Shivam V. Amin ◽  
Justin T. Roberts ◽  
Dillon G. Patterson ◽  
Alexander B. Coley ◽  
Jonathan A. Allred ◽  
...  

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