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Journal of Bacteriology, December 2008, p. 7786-7796, Vol. 190, No. 23
0021-9193/08/$08.00+0     doi:10.1128/JB.00715-08
Copyright © 2008, American Society for Microbiology. All Rights Reserved.

Processing of a Membrane Protein Required for Cell-to-Cell Signaling during Endospore Formation in Bacillus subtilis{triangledown}

Mónica Serrano,1 Filipe Vieira,1 Charles P. Moran Jr.,2 and Adriano O. Henriques1*

Instituto de Tecnologia Química e Biológica, Universidade Nova de Lisboa, Avenida da República, Apartado 127, 2781-901 Oeiras Codex, Portugal,1 Emory University School of Medicine, Department of Microbiology and Immunology, Atlanta, Georgia 303222

Received 21 May 2008/ Accepted 12 September 2008

Activation of the late prespore-specific RNA polymerase sigma factor {sigma}G during Bacillus subtilis sporulation coincides with completion of the engulfment process, when the prespore becomes a protoplast fully surrounded by the mother cell cytoplasm and separated from it by a double membrane system. Activation of {sigma}G also requires expression of spoIIIJ, coding for a membrane protein translocase of the YidC/Oxa1p/Alb3 family, and of the mother cell-specific spoIIIA operon. Here we present genetic and biochemical evidence indicating that SpoIIIAE, the product of one of the spoIIIA cistrons, and SpoIIIJ interact in the membrane, thereby linking the function of the spoIIIJ and spoIIIA loci in the activation of {sigma}G. We also show that SpoIIIAE has a functional Sec-type signal peptide, which is cleaved during sporulation. Furthermore, mutations that reduce or eliminate processing of the SpoIIIAE signal peptide arrest sporulation following engulfment completion and prevent activation of {sigma}G. SpoIIIJ-type proteins can function in cooperation with or independently of the Sec system. In one model, SpoIIIJ interacts with SpoIIIAE in the context of the Sec translocon to promote its correct localization and/or topology in the membrane, so that it can signal the activation of {sigma}G following engulfment completion.


* Corresponding author. Mailing address: Instituto de Tecnologia Química e Biológica, Universidade Nova de Lisboa, Avenida da República, Apartado 127, 2781-901 Oeiras Codex, Portugal. Phone: 351-21-4469521. Fax: 351-21-4411277. E-mail: aoh{at}itqb.unl.pt

{triangledown} Published ahead of print on 26 September 2008.


Journal of Bacteriology, December 2008, p. 7786-7796, Vol. 190, No. 23
0021-9193/08/$08.00+0     doi:10.1128/JB.00715-08
Copyright © 2008, American Society for Microbiology. All Rights Reserved.