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The coat morphogenetic protein SpoVID is necessary for spore encasement in Bacillus subtilis
Author(s) -
Wang Katherine H.,
Isidro Anabela L.,
Domingues Lia,
Eskandarian Haig A.,
McKenney Peter T.,
Drew Kevin,
Grabowski Paul,
Chua MingHsiu,
Barry Samantha N.,
Guan Michelle,
Bonneau Richard,
Henriques Adriano O.,
Eichenberger Patrick
Publication year - 2009
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/j.1365-2958.2009.06886.x
Subject(s) - bacillus subtilis , biology , spore , coat , coat protein , endospore , mutant , sporogenesis , microbiology and biotechnology , protein domain , biochemistry , bacteria , genetics , gene , rna , paleontology
Summary Endospores formed by Bacillus subtilis are encased in a tough protein shell known as the coat, which consists of at least 70 different proteins. We investigated the process of spore coat morphogenesis using a library of 40 coat proteins fused to green fluorescent protein and demonstrate that two successive steps can be distinguished in coat assembly. The first step, initial localization of proteins to the spore surface, is dependent on the coat morphogenetic proteins SpoIVA and SpoVM. The second step, spore encasement, requires a third protein, SpoVID. We show that in spoVID mutant cells, most coat proteins assembled into a cap at one side of the developing spore but failed to migrate around and encase it. We also found that SpoIVA directly interacts with SpoVID. A domain analysis revealed that the N‐terminus of SpoVID is required for encasement and is a structural homologue of a virion protein, whereas the C‐terminus is necessary for the interaction with SpoIVA. Thus, SpoVM, SpoIVA and SpoVID are recruited to the spore surface in a concerted manner and form a tripartite machine that drives coat formation and spore encasement.