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Journal of Bacteriology, March 2004, p. 1462-1474, Vol. 186, No. 5
0021-9193/04/$08.00+0     DOI: 10.1128/JB.186.5.1462-1474.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.

Assembly of an Oxalate Decarboxylase Produced under ^K Control into the Bacillus subtilis Spore Coat

Instituto de Tecnologia Química e Biológica, Universidade Nova de Lisboa, Apartado 127, 2781-901 Oeiras Codex,¹ Universidade Lusófona de Humanidades e Tecnologias, Departamento de Engenharias e Tecnologias, 1749-024 Lisbon, Portugal,⁵ Laboratory for Microbiology, Department of Biology, Philipps University of Marburg, D-35032 Marburg,² Max Planck Institute for Terrestrial Microbiology, D-35043 Marburg,³ Laboratory for Functional Genomics, Medical Faculty, Ernst Moritz Arndt University, D-17487 Greifswald, Germany⁴

Received 18 August 2003/ Accepted 25 November 2003

Over 30 polypeptides are synthesized at various times during sporulation in Bacillus subtilis, and they are assembled at the surface of the developing spore to form a multilayer protein structure called the coat. The coat consists of three main layers, an amorphous undercoat close to the underlying spore cortex peptidoglycan, a lamellar inner layer, and an electron-dense striated outer layer. The product of the B. subtilis oxdD gene was previously shown to have oxalate decarboxylase activity when it was produced in Escherichia coli and to be a spore constituent. In this study, we found that OxdD specifically associates with the spore coat structure, and in this paper we describe regulation of its synthesis and assembly. We found that transcription of oxdD is induced during sporulation as a monocistronic unit under the control of ^K and is negatively regulated by GerE. We also found that localization of a functional OxdD-green fluorescent protein (GFP) at the surface of the developing spore depends on the SafA morphogenetic protein, which localizes at the interface between the spore cortex and coat layers. OxdD-GFP localizes around the developing spore in a cotE mutant, which does not assemble the spore outer coat layer, but it does not persist in spores produced by the mutant. Together, the data suggest that OxdD-GFP is targeted to the interior layers of the coat. Additionally, we found that expression of a multicopy allele of oxdD resulted in production of spores with increased levels of OxdD that were able to degrade oxalate but were sensitive to lysozyme.

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