SpoIVB and CtpB Are Both Forespore Signals in the Activation of the Sporulation Transcription Factor σKinBacillus subtilis

• DOI: 10.1128/jb.00399-07
• Publication Date: 2007-06-09T04:56:59Z
• Authors: Nathalie Campo; David Z. Rudner
• Keywords: Spores, Bacterial; 0303 health sciences; 03 medical and health sciences; Bacterial Proteins; Serine Endopeptidases; Sigma Factor; Gene Expression Regulation, Bacterial; Bacillus subtilis; Signal Transduction; Transcription Factors

ABSTRACT The proteolytic activation of the mother cell transcription factor pro-σ K is controlled by a signal transduction pathway during sporulation in bacterium Bacillus subtilis . processing enzyme SpoIVFB, membrane-embedded metalloprotease, held inactive two other integral membrane proteins, SpoIVFA and BofA, that surrounds forespore. Two signaling serine proteases, SpoIVB CtpB, trigger cleaving regulatory protein SpoIVFA. absolutely required to activate derived from forespore compartment. CtpB necessary for proper timing σ was thought be signal. Here, we show ctpB gene expressed both compartments but synthesis under control G sufficient processing. We further cleaves vitro vivo this cleavage does not appear activation. Thus, proteins are made independently target same protein.