Abstract
The major outer membrane lipoprotein in Escherichia coli has provided a useful model for the studies of the biogenesis of bacterial lipoproteins in general. Lipoproteins with covalently linked glycerides and amide-linked fatty acids are present in both gram-negative and gram-positive bacteria. The primary structures and functions of these lipoproteins differ greatly but they share common features with respect to their modes of biosynthesis. They are first synthesized as precursor proteins, and in their precursor forms they are modified to become glyceride-modified prolipoproteins which are proteolytically processed by a unique prolipoprotein signal peptidase to form mature lipoproteins. This unique signal peptidase (signal peptidase II) is distinct from the signal peptidase for the processing of nonlipoprotein precursors (signal peptidase I) in its exquisite sensitivity to the cyclic antibiotic globomycin. Recent studies on the mechanism of export of prolipoprotein in E. coli and the specificities of the modification and processing enzymes are reviewed.
The outer membrane of gram-negative bacteria contains a few major proteins, one of which is the free-form of murein lipoprotein (Osborn and Wu, 1980). In the past 15 years since the discovery of the murein-bound lipoprotein by Braun and his coworkers, this major outer membrane lipoprotein has been one of the most thoroughly studied outer membrane proteins with respect to its structure, biosynthesis and assembly (Braun and Rehn, 1969; Braun, 1975). In 1977, Inouye and his coworkers identified a precursor form of the lipoprotein, the prolipoprotein, and determined the structure of the NH2-terminal signal sequence of prolipoprotein (Inouye et al., 1977). This timely discovery has provided a new dimension for the study of outer membrane lipoprotein, i.e., the mechanism of lipoprotein export in bacteria.
Studies in the last five years have revealed both unique and common features in the biogenesis of membrane lipoproteins in bacteria as compared to the export of proteins without covalently attached lipids (Silhavy et al., 1983). This paper summarizes recent advances in the studies of biogenesis of membrane lipoproteins in bacteria.
The biosynthesis and assembly of membrane lipoproteins in bacteria can be divided into discrete steps: synthesis of a prolipoprotein, insertion of the newly synthesized prolipoprotein into the cytoplasmic membrane, subsequent translocation across the cytoplasmic membrane, modifications and processing of the prolipoprotein, and in the case of the murein lipoprotein the intermembrane translocation and assembly of mature lipoprotein into the outer membrane of the cell envelope.
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© 1984 Plenum Press, New York
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Wu, H.C. (1984). Biogenesis of Membrane Lipoproteins in Bacteria. In: Haber, E. (eds) The Cell Membrane. Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-1215-4_3
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DOI: https://doi.org/10.1007/978-1-4684-1215-4_3
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