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A LysM Domain Intervenes in Sequential Protein-Protein and Protein-Peptidoglycan Interactions Important for Spore Coat Assembly in Bacillus subtilis
Author(s) -
Maria de Fátima Pereira,
Filipa Nunes,
Fernando Cruz,
Catarina G. Fernandes,
Anabela Isidro,
Diana Lousa,
Cláudio M. Soares,
Charles P. Moran,
Adriano O. Henriques,
Mónica Serrano
Publication year - 2018
Publication title -
journal of bacteriology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.652
H-Index - 246
eISSN - 1067-8832
pISSN - 0021-9193
DOI - 10.1128/jb.00642-18
Subject(s) - peptidoglycan , bacillus subtilis , biology , microbiology and biotechnology , multiprotein complex , protein domain , scaffold protein , biochemistry , cell wall , genetics , bacteria , signal transduction , gene
Bacillus subtilis spores are encased in a multiprotein coat that surrounds an underlying peptidoglycan layer, the cortex. How the connection between the two layers is enforced is not well established. Here, we elucidate the role of the peptidoglycan-binding LysM domain, present in two proteins, SafA and SpoVID, that govern the localization of additional proteins to the coat. We found that SafALysM is a protein-protein interaction module during the early stages of coat assembly and a cortex-binding module at late stages in morphogenesis, with the cortex-binding function promoting a tight connection between the cortex and the coat. In contrast, SpoVIDLysM functions only as a protein-protein interaction domain that targets SpoVID to the spore surface at the onset of coat assembly.

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