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Diverse supramolecular structures formed by self‐assembling proteins of the B acillus subtilis spore coat
Author(s) -
Jiang Shuo,
Wan Qiang,
Krajcikova Daniela,
Tang Jilin,
Tzokov Svetomir B.,
Barak Imrich,
Bullough Per A.
Publication year - 2015
Publication title -
molecular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.857
H-Index - 247
eISSN - 1365-2958
pISSN - 0950-382X
DOI - 10.1111/mmi.13030
Subject(s) - bacillus subtilis , biology , spore , endospore , supramolecular chemistry , superstructure , bacterial spore , spore germination , microbiology and biotechnology , biophysics , bacteria , crystallography , chemistry , genetics , oceanography , crystal structure , geology
Summary Bacterial spores (endospores), such as those of the pathogens C lostridium difficile and B acillus anthracis , are uniquely stable cell forms, highly resistant to harsh environmental insults. B acillus subtilis is the best studied spore‐former and we have used it to address the question of how the spore coat is assembled from multiple components to form a robust, protective superstructure. B . subtilis coat proteins ( CotY , CotE , CotV and CotW ) expressed in E scherichia coli can arrange intracellularly into highly stable macro‐structures through processes of self‐assembly. Using electron microscopy, we demonstrate the capacity of these proteins to generate ordered one‐dimensional fibres, two‐dimensional sheets and three‐dimensional stacks. In one case ( CotY ), the high degree of order favours strong, cooperative intracellular disulfide cross‐linking. Assemblies of this kind could form exquisitely adapted building blocks for higher‐order assembly across all spore‐formers. These physically robust arrayed units could also have novel applications in nano‐biotechnology processes.