Unique Degradation Signal for ClpCP in Bacillus subtilis

AUTOR(ES)
FONTE

American Society for Microbiology

RESUMO

Regulation of the cell-specific transcription factor σF in the spore-forming bacterium Bacillus subtilis involves the antisigma factor SpoIIAB. Contributing to the activation of σF 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.

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