Abstract
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.
Keywords:
Staphylococcusaureus; Type VII secretion; membrane protein complex; protein secretion.
© 2016 Federation of European Biochemical Societies.
Publication types
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Comparative Study
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Research Support, Non-U.S. Gov't
MeSH terms
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Bacterial Proteins / chemistry
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Bacterial Proteins / genetics
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Bacterial Proteins / metabolism*
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Cross-Linking Reagents / chemistry
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Detergents / chemistry
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Digitonin / chemistry
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Dimerization
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Formaldehyde / chemistry
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Gene Deletion
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Glucosides / chemistry
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Models, Biological*
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Molecular Weight
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Native Polyacrylamide Gel Electrophoresis
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Octoxynol / chemistry
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Open Reading Frames
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Phosphorylcholine / analogs & derivatives
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Phosphorylcholine / chemistry
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Polymers / chemistry
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Recombinant Fusion Proteins / chemistry
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Recombinant Fusion Proteins / metabolism
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Recombinant Proteins / chemistry
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Recombinant Proteins / metabolism
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Solubility
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Staphylococcus aureus / metabolism*
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Succinimides / chemistry
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Type VII Secretion Systems / chemistry
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Type VII Secretion Systems / genetics
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Type VII Secretion Systems / metabolism*
Substances
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Bacterial Proteins
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Cross-Linking Reagents
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Detergents
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Glucosides
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Polymers
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Recombinant Fusion Proteins
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Recombinant Proteins
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Succinimides
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Type VII Secretion Systems
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Phosphorylcholine
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Formaldehyde
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dodecylphosphocholine
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dodecyl maltoside
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Octoxynol
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Digitonin
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disuccinimidyl suberate
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paraform