Sigma factors from E. coli, B. subtilis, phage SP01, and phage T4 are homologous proteins.
We show, using dot matrix comparisons and statistical analysis of sequence alignments, that seven sequenced sigma factors, E. coli sigma-70 and sigma-32, B. subtilis sigma-43 and sigma-29, phage SP01 gene products 28 and 34, and phage T4 gene product 55, comprise a homologous family of proteins. Sigma-70, sigma-32, and sigma-43 each have two copies of a sequence similar to the helix-turn-helix DNA binding motif seen in CRP, and lambda repressor and cro proteins. B. subtilis sigma-29, SP01 gp28, and SP01 gp34 have at least one copy similar to this sequence. We propose that a second sequence, conserved in all seven proteins is the core RNA polymerase binding site. A third region, present only in sigma-70 and sigma-43, may also be involved in interaction with core. Available mutational evidence supports our model for sigma factor structure.
D000595:Amino Acid Sequence; D001412:Bacillus subtilis / Q000235:genetics*; D001435:Bacteriophages / Q000235:genetics*; D001665:Binding Sites; D012321:DNA-Directed RNA Polymerases / Q000378:metabolism; D004926:Escherichia coli / Q000235:genetics*; D009154:Mutation; D011485:Protein Binding; D012808:Sigma Factor / Q000235:genetics*; D013045:Species Specificity; D013604:T-Phages / Q000235:genetics*; D014157:Transcription Factors / Q000235:genetics*
D012808:Sigma Factor; D014157:Transcription Factors; D012321:DNA-Directed RNA Polymerases