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Processing by inverted plasma membrane vesicles of in vitro synthesized major lipoprotein from Escherichia coli
Author(s) -
Krishnabhakdi Siegfried S.,
Müller Matthias
Publication year - 1988
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(88)80710-5
Subject(s) - vesicle , escherichia coli , biochemistry , signal peptidase , signal peptide , lipoprotein , chemistry , membrane , in vitro , biology , cholesterol , peptide sequence , gene
Synthesis, lipid modification and proteolytic processing of the major lipoprotein from Escherichia coli is shown to occur in a homologous in vitro transcription‐translation system containing inverted plasma membrane vesicles. The primary translation product (cross‐reacting with anti‐lipoprotein antiserum) is a precursor which is converted into a lower molecular mass species of the size of mature lipoprotein by the addition of inverted membrane vesicles from E. coli . Conversion is prevented by globomycin, a specific inhibitor of the unique lipoprotein‐signal peptidase II, which is active only on lipid‐containing precursors. The inverted plasma membrane vesicles used here must therefore contain active lipid‐modifying enzymes and signal peptidase II.