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Journal of Bacteriology, March 2001, p. 2032-2040, Vol. 183, No. 6
0021-9193/01/$04.00+0   DOI: 10.1128/JB.183.6.2032-2040.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

Alternative Translation Initiation Produces a Short Form of a Spore Coat Protein in Bacillus subtilis

Amanda J. Ozin,1 Teresa Costa,2 Adriano O. Henriques,2 and Charles P. Moran Jr.1,*

Department of Microbiology and Immunology, Emory University School of Medicine, Atlanta, Georgia 30322,1 and Instituto de Tecnologia Química e Biológica, Universidade Nova de Lisboa, 2781-901 Oeiras Codex, Portugal2

Received 25 September 2000/Accepted 20 December 2000

During endospore formation in Bacillus subtilis, over two dozen polypeptides are localized to the developing spore and coordinately assembled into a thick multilayered structure called the spore coat. Assembly of the coat is initiated by the expression of morphogenetic proteins SpoIVA, CotE, and SpoVID. These morphogenetic proteins appear to guide the assembly of other proteins into the spore coat. For example, SpoVID forms a complex with the SafA protein, which is incorporated into the coat during the early stages of development. At least two forms of SafA are found in the mature spore coat: a full-length form and a shorter form (SafA-C30) that begins with a methionine encoded by codon 164 of safA. In this study, we present evidence that the expression of SafA-C30 arises from translation initiation at codon 164. We found only a single transcript driving expression of SafA. A stop codon engineered just upstream of a predicted ribosome-binding site near codon M164 abolished formation of full-length SafA, but not SafA-C30. The same effect was observed with an alanine substitution at codon 1 of SafA. Accumulation of SafA-C30 was blocked by substitution of an alanine codon at codon 164, but not by a substitution at a nearby methionine at codon 161. We found that overproduction of SafA-C30 interfered with the activation of late mother cell-specific transcription and caused a strong sporulation block.

* Corresponding author. Mailing address: Department of Microbiology and Immunology, Emory University School of Medicine, 3001 Rollins Research Center, Atlanta, GA 30322. Phone: (404) 727-5969. Fax: (404) 727-3659. E-mail: moran{at}microbio.emory.edu.

Journal of Bacteriology, March 2001, p. 2032-2040, Vol. 183, No. 6
0021-9193/01/$04.00+0   DOI: 10.1128/JB.183.6.2032-2040.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.


This article has been cited by other articles:

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