A microdomain for protein secretion in Gram-positive bacteria.
Gram-positive bacteria face unique challenges in generating biologically active conformations for their exported proteins because they lack a dedicated compartment for folding secreted polypeptides. We have discovered that protein secretion by way of the general secretory (Sec) pathway in the important human pathogen Streptococcus pyogenes proceeds through a single microdomain. Unlike other mechanisms for asymmetry involving the Sec pathway, proteins destined for secretion are targeted to a single locus distal to either cell pole that has specialized to contain the Sec translocons. This subcellular organization may represent a paradigm for secretion common to other Gram-positive pathogens with profound implications for pathogenesis.
Rosch
Jason
J
Department of Molecular Microbiology, Washington University School of Medicine, Box 8230, St. Louis, MO 63110-1093, USA.
Caparon
Michael
M
D001426:Bacterial Proteins / Q000737:chemistry / Q000276:immunology / Q000378:metabolism*; D002462:Cell Membrane / Q000378:metabolism* / Q000648:ultrastructure; D002473:Cell Wall / Q000378:metabolism; D003546:Cysteine Endopeptidases / Q000737:chemistry / Q000276:immunology / Q000378:metabolism*; D007106:Immune Sera; D007150:Immunohistochemistry; D021962:Membrane Microdomains / Q000378:metabolism* / Q000648:ultrastructure; D016253:Microscopy, Immunoelectron; D017510:Protein Folding; D021381:Protein Transport; D013297:Streptococcus pyogenes / Q000378:metabolism* / Q000648:ultrastructure
D001426:Bacterial Proteins; D007106:Immune Sera; D003546:Cysteine Endopeptidases; C042477:streptopain