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Interaction between Coat Morphogenetic Proteins SafA and SpoVID

Teresa Costa,^1, Anabela L. Isidro,¹ Charles P. Moran Jr.,² and Adriano O. Henriques^1*

Instituto de Tecnologia Química e Biológica, Universidade Nova de Lisboa, Avenida da República, EAN, 2781-157 Oeiras, Portugal,¹ Emory University School of Medicine, Department of Microbiology and Immunology, 3010 Rollins Research Center, Atlanta, Georgia 30322²

Received 26 May 2006/ Accepted 23 August 2006

Morphogenetic proteins such as SpoVID and SafA govern assembly of the Bacillus subtilis endospore coat by guiding the various protein structural components to the surface of the developing spore. Previously, a screen for peptides able to interact with SpoVID led to the identification of a PYYH motif present in the C-terminal half of the SafA protein and to the subsequent demonstration that SpoVID and SafA directly interact. spoVID and safA spores show deficiencies in coat assembly and are lysozyme susceptible. Both proteins, orthologs of which are found in all Bacillus species, have LysM domains for peptidoglycan binding and localize to the cortex-coat interface. Here, we show that the interaction between SafA and SpoVID involves the PYYH motif (region B) but also a 13-amino-acid region (region A) just downstream of the N-terminal LysM domain of SafA. We show that deletion of region B does not block the interaction of SafA with SpoVID, nor does it bring about spore susceptibility to lysozyme. Nevertheless, it appears to reduce the interaction and affects the complex. In contrast, lesions in region A impaired the interaction of SafA with SpoVID in vitro and, while not affecting the accumulation of SafA in vivo, interfered with the localization of SafA around the developing spore, causing aberrant assembly of the coat and lysozyme sensitivity. A peptide corresponding to region A interacts with SpoVID, suggesting that residues within this region directly contact SpoVID. Since region A is highly conserved among SafA orthologs, this motif may be an important determinant of coat assembly in the group of Bacillus spore formers.

Published ahead of print on 1 September 2006.

Present address: Department of Molecular, Cellular, and Developmental Biology, Yale University, New Haven, CT 06520.