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SpoIVB‐mediated cleavage of SpoIVFA could provide the intercellular signal to activate processing of Pro‐σ K in Bacillus subtilis
Author(s) -
Dong Tran C.,
Cutting Simon M.
Publication year - 2003
Publication title -
molecular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.857
H-Index - 247
eISSN - 1365-2958
pISSN - 0950-382X
DOI - 10.1046/j.1365-2958.2003.03651.x
Subject(s) - bacillus subtilis , biology , cleavage (geology) , microbiology and biotechnology , signal peptidase , intracellular , signal peptide , zinc finger , serine , signal transduction , metalloproteinase , biochemistry , biophysics , transcription factor , gene , enzyme , phosphorylation , peptide sequence , genetics , bacteria , paleontology , fracture (geology)
Summary SpoIVB is the critical determinant for intercompartmental signalling of pro‐σ K processing during sporulation in Bacillus subtilis . We show here that the SpoIVB serine peptidase can cleave the SpoIVFA protein, which is one component of the pro‐σ K processing complex. SpoIVFA has been shown elsewhere (Rudner, D.Z., and Losick, R., 2002, Genes Dev 16: 1007–1018) to tether BofA and SpoIVFB in a membrane‐embedded heteroligomeric complex in which BofA directly inhibits the activity of SpoIVFB. Cleavage of SpoIVFA would provide the necessary signal to dissolve this complex and release BofA‐mediated inhibition on the zinc metalloprotease, SpoIVFB, that is responsible for cleaving pro‐σ K to its mature form. We also show that the SpoIVB PDZ domain is required for self‐recognition and trans cleavage of SpoIVB and is probably also used to target an internal motif within the C‐terminal region of SpoIVFA exposed in the space between the inner and outer forespore membranes. This work reveals the mechanism of intercompartmental signalling and provides a unified model as to how σ K ‐directed gene expression in the mother cell is co‐ordinated with events in the forespore chamber.