In vitro assembly of membrane on the entire surface of peptidoglycan sacculus from dissociated components of the outer membrane of Escherichia coli has been achieved. When the outer membrane dissociated in sodium dodecyl sulfate solution was mixed with the lipoprotein-bearing peptidoglycan sacculi and dialyzed against magnesium chloride solution, only large membranous sacculi were formed.The size and shape of the membrane formed were similar to those of the peptidoglycan sacculi used When the peptidoglycan sacculi were replaced by sonicated fragments of the peptidoglycan, the size and shape of the membranes formed were similar to those of the fragmented peptidoglycan.Membranous vesicles resembl ing the original outer membrane preparation were recovered when the assembled membranepeptidoglycan complex was fragmented bybrief sonication and treated with lysozyme. When lipoprotein-free peptidoglycan sacculi were used, only small membranous vesicles resembling the original outer membrane preparation were formed, leaving the peptidoglycan sacculus as it was. Lipopolysaccharide, phospholipid or a mixture of them can be assembled into membranous structures preferentially on the peptidoglycan sacculi; lipoprotein covalently bound to the peptidoglycan sacculi was again essential for the assembly However, the assembled membranes were often multilaminar and were not as clear and complete as those formed with all membrane components, including proteins.
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Yamada et al. (1977) studied this question.