Abstract
Regulation of the cell-specific transcription factor sigma(F) in the spore-forming bacterium Bacillus subtilis involves the antisigma factor SpoIIAB. Contributing to the activation of sigma(F) is the degradation of SpoIIAB in a manner that depends on the protease ClpCP. Here we show that the three residues (LCN) located at the extreme C terminus of SpoIIAB are both necessary and sufficient for this degradation. We also report that the use of the LCN extension as a degradation signal for ClpCP is unique to SpoIIAB.
MeSH Terms
Adenosine Triphosphatases/genetics,metabolism
Bacillus subtilis/genetics,metabolism,physiology
Bacterial Proteins/chemistry,genetics,metabolism
Endopeptidase Clp
Gene Expression Regulation, Bacterial
Heat-Shock Proteins/genetics,metabolism
Serine Endopeptidases/genetics,metabolism
Signal Transduction
Spores, Bacterial/physiology
Chemicals
Bacterial Proteins
ClpC protein, Bacteria
Heat-Shock Proteins
SpoIIB protein, Bacillus subtilis
spore-specific proteins, Bacillus
Serine Endopeptidases
Endopeptidase Clp
Adenosine Triphosphatases
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Pan Qi
Department of Molecular and Cellular Biology, Harvard University, 16 Divinity Avenue, Cambridge, MA 02138, USA.
Losick Richard
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