Spores formed by Bacillus subtilis are surrounded by a protective and multilayered shell, termed the coat, which grants the spores resistance to various environmental stresses and facilitates spore germination. The spore coat consists of more than seventy different proteins, arranged into at least four distinct structural layers: the undercoat, inner coat, outer coat and crust. However, how these proteins, especially the morphogenetic proteins, interact to establish the organized, functional coat layers remains poorly understood. CotY and CotZ as the components of the crust, play a morphogenetic role in the crust assembly around the spore. In this study, the single molecule force spectroscopy was used to investigate the interaction and dynamics between CotY and CotZ at the single-molecule level. The results show that homotypic interactions of CotY and CotZ and the heterotypic interaction between CotY and CotZ exist. Furthermore, the dissociation kinetics of the complexes were studied by monitoring the relationship between the unbinding forces and the loading rates at different pulling velocities. In this way, a series of kinetic parameters regarding the three different complexes were obtained. It revealed the strong interactions between CotY and CotZ, CotY and CotY, and a relatively weak interaction of CotZ and CotZ.
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Article Synopsis
- - Bacillus subtilis spores have a robust structure with a thick protein layer called the spore coat, made up of over 80 proteins organized into four layers: basement, inner coat, outer coat, and crust.
- - During spore development, proteins from the cytoplasm are deposited onto the prespore surface, with certain morphogenetic proteins forming a scaffold for the other proteins.
- - This study used a bacterial two-hybrid system to explore interactions among proteins in the outer coat and crust, revealing self-interactions and novel contacts that could help clarify the roles of proteins like CotE, CotY, and CotZ in spore coat development.
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