Rosch Jason W, Hsu Fong Fu, Caparon Michael G
Department of Molecular Microbiology, Washington University School of Medicine, Box 8230, 660 S. Euclid Ave. no. 8230, St. Louis, MO 63110-1093, USA.
J Bacteriol. 2007 Feb;189(3):801-6. doi: 10.1128/JB.01549-06. Epub 2006 Dec 1.
The ExPortal of Streptococcus pyogenes is a membrane microdomain dedicated to the secretion and folding of proteins. We investigated the lipid composition of the ExPortal by examining the distribution of anionic membrane phospholipids. Staining with 10-N-nonyl-acridine orange revealed a single microdomain enriched with an anionic phospholipid whose staining characteristics and behavior in a cardiolipin-deficient mutant were characteristic of phosphatidylglycerol. Furthermore, the location of the microdomain corresponded to the site of active protein secretion at the ExPortal. These results indicate that the ExPortal is an asymmetric lipid microdomain, whose enriched content of anionic phospholipids may play an important role in ExPortal organization and protein trafficking.
化脓性链球菌的外排门户是一个专门负责蛋白质分泌和折叠的膜微区。我们通过检测阴离子膜磷脂的分布来研究外排门户的脂质组成。用10-N-壬基吖啶橙染色显示有一个富含阴离子磷脂的单一微区,其染色特征以及在缺乏心磷脂的突变体中的行为具有磷脂酰甘油的特点。此外,该微区的位置与外排门户处活性蛋白分泌的位点相对应。这些结果表明,外排门户是一个不对称的脂质微区,其富含的阴离子磷脂可能在外排门户的组织和蛋白质运输中发挥重要作用。