SpoIVB and CtpB Are Both Forespore Signals in the Activation of the Sporulation Transcription Factor σKinBacillus subtilis
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
DOI:
10.1128/jb.00399-07
Publication Date:
2007-06-09T04:56:59Z
AUTHORS (2)
ABSTRACT
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.
SUPPLEMENTAL MATERIAL
Coming soon ....
REFERENCES (36)
CITATIONS (35)
EXTERNAL LINKS
PlumX Metrics
RECOMMENDATIONS
FAIR ASSESSMENT
Coming soon ....
JUPYTER LAB
Coming soon ....