Unique degradation signal for ClpCP in Bacillus subtilis.
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.
Pan
Qi
Q
Department of Molecular and Cellular Biology, Harvard University, 16 Divinity Avenue, Cambridge, MA 02138, USA.
Losick
Richard
R
D000251:Adenosine Triphosphatases / Q000235:genetics / Q000378:metabolism*; D001412:Bacillus subtilis / Q000235:genetics / Q000378:metabolism* / Q000502:physiology; D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D049071:Endopeptidase Clp; D015964:Gene Expression Regulation, Bacterial; D006360:Heat-Shock Proteins / Q000235:genetics / Q000378:metabolism*; D012697:Serine Endopeptidases / Q000235:genetics / Q000378:metabolism*; D015398:Signal Transduction; D013171:Spores, Bacterial / Q000502:physiology
D001426:Bacterial Proteins; C087481:ClpC protein, Bacteria; D006360:Heat-Shock Proteins; C095877:SpoIIB protein, Bacillus subtilis; C030069:spore-specific proteins, Bacillus; D012697:Serine Endopeptidases; D049071:Endopeptidase Clp; D000251:Adenosine Triphosphatases