A carboxy-terminal 16-amino-acid region of s38 of Escherichia coli is important for transcription under high-salt conditions and sigma activities in vivo

Ohnuma, M.; Fujita, N.; Ishihama, A.

Journal of Bacteriology 182(16): 28-31


ISSN/ISBN: 0021-9193
Accession: 009747541

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The function of the extreme C-terminal 16-amino-acid region of the sigma subunit of RNA polymerase in Escherichia coli, s38, was investigated. The C-terminal 16-amino-acid region of s38 from residues 315-30 is well conserved among the rpoS gene products of enteric bacteria. Truncation of the region using promoter-lacZ constructs led to the loss of sigma activity in vivo; however, the mutant s38 kept the binding activity in vivo to the core system. Furthermore, in vitro transcription analysis revealed that, under high potassium glutamate concentrations, s38 holoenzyme transcription activity was significantly reduced by the truncation of the C-terminal tail element.