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Membrane interactions and self‐association of components of the Ess/Type VII secretion system of Staphylococcus aureus
Author(s) -
Jäger Franziska,
Zoltner Martin,
Kneuper Holger,
Hunter William N.,
Palmer Tracy
Publication year - 2016
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1002/1873-3468.12065
Subject(s) - homomeric , secretion , staphylococcus aureus , virulence , microbiology and biotechnology , chemistry , membrane protein , biology , membrane , gene , biochemistry , bacteria , genetics , protein subunit
The Ess/Type VII protein secretion system, essential for virulence of pathogenic Staphylococcus aureus , is dependent upon the four core membrane proteins EssA, EssB, EssC and EsaA. Here, we use crosslinking and blue native PAGE analysis to show that the EssB, EssC and EsaA proteins individually form homomeric complexes. Surprisingly, these components appear unable to interact with each other, or with the EssA protein. We further show that two high molecular weight multimers of EssC detected in whole cells are not dependent upon the presence of EsxA, EsxB or any other Ess component for their assembly.