Article
Structural and functional properties of a Bacillus subtilis temperature-sensitive sigma(A) factor.
Proteins - 1 Sept 2000
Wen Y D, Liao C T, Liou K M, Wang W H, Huang W C, Chang B Y
Abstract excerpt
Bacillus subtilis DB1005 is a temperature-sensitive (Ts) sigA mutant containing double-amino-acid substitutions (I198A and I202A) on the hydrophobic face of the promoter -10 binding helix of sigma(A) factor. We have analyzed the structural and functional properties of this mutant sigma(A) factor both in vivo and in vitro. Our data revealed that the Ts sigma(A) factor possessed predominantly a multimeric structure...
Topics
- Amino Acid Substitution
- Bacillus subtilis
- Chromatography, Gel
- Electrophoresis, Polyacrylamide Gel
- Mutation
- Protein Binding
- Protein Denaturation
- Sigma Factor
- Spectrometry, Fluorescence
- Temperature
- Transcription, Genetic
