Lipid-synthesis-dependent biosynthesis (or assembly) of major outer-membrane proteins of Escherichia coli.
Upon inhibition of fatty acid synthesis in the presence of cerulenin, the uptake of 5' AMP and of other nutrients using similar pore systems can be inhibited as much as 70%. The same effect was observed upon inhibition of phospholipid synthesis after glycerol deprivation in a mutant strain defective in sn-glycerol-3-phosphate acyltransferase. Resumption of both fatty acid synthesis and phospholipid synthesis restores a normal uptake of 5' AMP. The protein composition of the outer membranes, analyzed after pulse radiolabelling by [35S]methionine, was mainly altered in OmpF and OmpC proteins. These proteins are the main porins used by most nutrients like 5' AMP. Whereas the synthesis or the assembly of OmpF protein seems to be more inhibited that that of OmpC protein after inhibition of fatty acid synthesis, the reverse case was observed after inhibition of phospholipid synthesis. No protein produced during inhibition of fatty-acid or phospholipid synthesis is reincorporated into the outer membrane after resumption of these syntheses. These results are discussed with regard to the biosynthesis and assembly of these proteins.
D000249:Adenosine Monophosphate / Q000378:metabolism; D001692:Biological Transport / Q000187:drug effects; D002462:Cell Membrane / Q000187:drug effects / Q000378:metabolism; D002569:Cerulenin / Q000494:pharmacology; D004926:Escherichia coli / Q000187:drug effects / Q000378:metabolism*; D005227:Fatty Acids / Q000096:biosynthesis*; D005230:Fatty Acids, Nonesterified / Q000494:pharmacology; D005990:Glycerol / Q000378:metabolism; D007700:Kinetics; D008565:Membrane Proteins / Q000096:biosynthesis*; D010743:Phospholipids / Q000096:biosynthesis
D005227:Fatty Acids; D005230:Fatty Acids, Nonesterified; D008565:Membrane Proteins; D010743:Phospholipids; D002569:Cerulenin; D000249:Adenosine Monophosphate; D005990:Glycerol