Translocation of phospholipids from the inner to the outer membrane of Escherichia coli.
نویسندگان
چکیده
The translocation of lipids from the inner to the outer membrane of Escherichia coli has been investigated by pulse-chase experiments. After a pulse with [2-3H]glycerol, the specific activity of the newly synthesized [3H]phosphatidylethanolamine was 5 times greater in the inner than in the outer membrane. During the chase, [3H]phosphatidylethanolamine was translocated to the outer membrane. At 37 degrees C, the half-life for translocation was 2.8 min. This rate was not influenced by alteration in the cellular growth rate at 37 degrees C. Altering the cellular growth temperature had a pronounced effect on the rate of phosphatidylethanolamine translocation. Energy inhibitors that deplete the protonmotive force markedly inhibited the translocation. Translocation was not affected by inhibitors of ATP, protein, or lipid synthesis. Phosphatidylglycerol and cardiolipin are transfocated very rapidly, with half-lives shorter than 30 sec.
منابع مشابه
SDS-PAGE Analysis of the Outer Membrane Proteins of Uropathogenic Escherichia coli Isolated from Patients in Different Wards of Nemazee Hospital, Shiraz, Iran
Background: Outer membrane proteins (OMPs) constitute the main structure and about half of the cell wall of Gram-negative bacteria. The OMPs of Escherichia coli (E. coli) play an important role in its drug resistance. Previous studies have shown that the OMPs of E. coli enhance its pathogenic effects by helping the bacterium to evade the immune defense and promote its adsorption to host cells. ...
متن کاملPeriplasmic expression of Bacillus thermocatenulatus lipase in Escherichia coli in presence of different signal sequences
Efforts to express lipase in the periplasmic space of Escherichia coli have so far been unsuccessful andmost of the expressed recombinant lipases accumulate in the insoluble cell fraction. To evaluate the role ofnative and heterologous signal peptides in translocation of the lipase across the inner membrane of E. coli,the lipase gene (btl2) was cloned downstream of the native ...
متن کاملImmunogenicity of enterotoxigenic Escherichia coli outer membrane vesicles encapsulated in chitosan nanoparticles
Objective(s): Enterotoxigenic Escherichia coli (ETEC) is an important cause of diarrheal disease in humans, particularly in children under 5 years and travelers in developing countries. To our knowledge, no vaccine is licensed yet to protect against ETEC infection. Like many Gram-negative pathogens, ETEC can secrete outer membrane vesicles (OMVs). These structures contain various immunogenic vi...
متن کاملPhosphoglycerides and phospholipase C in membrane fractions of Escherichia coli B.
The phospholipid composition and the phospholipase C activity of envelope fractions of Escherichia coli B were determined with special consideration of fractions containing sites at which an attachment of inner and outer membranes had been observed in the electron microscope (Int.M). Phosphoglycerides labeled with [14C]palmitic acid and [3H]serine were extracted from membrane fractions and iden...
متن کاملThe reconstituted Escherichia coli MsbA protein displays lipid flippase activity
The MsbA protein is an essential ABC (ATP-binding-cassette) superfamily member in Gram-negative bacteria. This 65 kDa membrane protein is thought to function as a homodimeric ATP-dependent lipid translocase or flippase that transports lipid A from the inner to the outer leaflet of the cytoplasmic membrane. We have previously shown that purified MsbA from Escherichia coli displays high ATPase ac...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید
ثبت ناماگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید
ورودعنوان ژورنال:
- Proceedings of the National Academy of Sciences of the United States of America
دوره 77 4 شماره
صفحات -
تاریخ انتشار 1980