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Journal of Bacteriology, October 2003, p. 6051-6056, Vol. 185, No. 20
0021-9193/03/$08.00+0     DOI: 10.1128/JB.185.20.6051-6056.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.

A Second PDZ-Containing Serine Protease Contributes to Activation of the Sporulation Transcription Factor ^K in Bacillus subtilis

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

Received 8 May 2003/ Accepted 1 August 2003

Gene expression late during the process of sporulation in Bacillus subtilis is governed by a multistep, signal transduction pathway involving the transcription factor ^K, which is derived by regulated proteolysis from the inactive proprotein pro-^K. Processing of pro-^K is triggered by a signaling protein known as SpoIVB, a serine protease that contains a region with similarity to the PDZ family of protein-protein interaction domains. Here we report the discovery of a second PDZ-containing serine protease called CtpB that contributes to the activation of the pro-^K processing pathway. CtpB is a sporulation-specific, carboxyl-terminal processing protease and shares several features with SpoIVB. We propose that CtpB acts to fine-tune the regulation of pro-^K processing, and we discuss possible models by which CtpB influences the ^K activation pathway.

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