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Journal of Bacteriology, September 2003, p. 5275-5278, Vol. 185, No. 17
0021-9193/03/$08.00+0     DOI: 10.1128/JB.185.17.5275-5278.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.

Unique Degradation Signal for ClpCP in Bacillus subtilis

Qi Pan and Richard Losick*

Department of Molecular and Cellular Biology, Harvard University, Cambridge, Massachusetts 02138

Received 15 April 2003/ Accepted 4 June 2003

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.

* Corresponding author. Mailing address: Department of Molecular and Cellular Biology, Harvard University, 16 Divinity Ave., Cambridge, MA 02138. Phone: (617) 495-4905. Fax: (617) 496-4642. E-mail: losick{at}mcb.harvard.edu.

Journal of Bacteriology, September 2003, p. 5275-5278, Vol. 185, No. 17
0021-9193/03/$08.00+0     DOI: 10.1128/JB.185.17.5275-5278.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.



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