title: Membrane interactions and self-association of components of the Ess/Type VII secretion system of Staphylococcus aureus.
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.
authors.affiliation: Divisions of Molecular Microbiology, School of Life Sciences, University of Dundee, Dundee, UK.
authors.forename: Franziska
authors.initials: F
authors.lastname: Jäger
authors.affiliation: Biological Chemistry and Drug Discovery, School of Life Sciences, University of Dundee, Dundee, UK.
authors.forename: Martin
authors.initials: M
authors.lastname: Zoltner
authors.affiliation: Divisions of Molecular Microbiology, School of Life Sciences, University of Dundee, Dundee, UK.
authors.forename: Holger
authors.initials: H
authors.lastname: Kneuper
authors.affiliation: Biological Chemistry and Drug Discovery, School of Life Sciences, University of Dundee, Dundee, UK.
authors.forename: William N
authors.initials: WN
authors.lastname: Hunter
authors.affiliation: Divisions of Molecular Microbiology, School of Life Sciences, University of Dundee, Dundee, UK.
authors.forename: Tracy
authors.initials: T
authors.lastname: Palmer
mesh_terms: D001426:Bacterial Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D003432:Cross-Linking Reagents / Q000737:chemistry; D003902:Detergents / Q000737:chemistry; D004072:Digitonin / Q000737:chemistry; D019281:Dimerization; D005557:Formaldehyde / Q000737:chemistry; D017353:Gene Deletion; D005960:Glucosides / Q000737:chemistry; D008954:Models, Biological; D008970:Molecular Weight; D063347:Native Polyacrylamide Gel Electrophoresis; D017830:Octoxynol / Q000737:chemistry; D016366:Open Reading Frames; D010767:Phosphorylcholine / Q000031:analogs & derivatives / Q000737:chemistry; D011108:Polymers / Q000737:chemistry; D011993:Recombinant Fusion Proteins / Q000737:chemistry / Q000378:metabolism; D011994:Recombinant Proteins / Q000737:chemistry / Q000378:metabolism; D012995:Solubility; D013211:Staphylococcus aureus / Q000378:metabolism*; D013388:Succinimides / Q000737:chemistry; D000069377:Type VII Secretion Systems / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*
chemical_list: D001426:Bacterial Proteins; D003432:Cross-Linking Reagents; D003902:Detergents; D005960:Glucosides; D011108:Polymers; D011993:Recombinant Fusion Proteins; D011994:Recombinant Proteins; D013388:Succinimides; D000069377:Type VII Secretion Systems; D010767:Phosphorylcholine; D005557:Formaldehyde; C028810:dodecylphosphocholine; C040358:dodecyl maltoside; D017830:Octoxynol; D004072:Digitonin; C019358:disuccinimidyl suberate; C003043:paraform
keywords: Staphylococcusaureus; Type VII secretion; membrane protein complex; protein secretion