Post-translational modification and processing of outer membrane prolipoproteins in Escherichia coli
- 1 January 1984
- journal article
- review article
- Published by Springer Nature in Molecular and Cellular Biochemistry
- Vol. 60 (1), 5-15
- https://doi.org/10.1007/bf00226297
Abstract
This mini review is primarily concerned with the biosynthesis of the major outer membrane lipoprotein of Escherichia coli. The lipoprotein is composed of fifty-eight amino acid residues, one glyceride residue and one acyl residue being at the amino terminal cysteine residue. About one-third of the lipoprotein is covalently bound to the underlying peptidoglycan layer and plays an important role in the assembly of the outer membrane on the peptidoglycan layer. The lipoprotein is first synthesized on ribosomes as a precursor form having twenty extra amino acid residues (signal peptide) at the amino terminus. During secretion through the cytoplasmic membrane, the modification at the cysteine residue that is to be the amino terminus of the mature lipoprotein and cleavage of the signal peptide take place successively. These events are then followed by N-acetylation of the terminal cysteine residue, translocation to the outer membrane, and covalent binding to the peptidoglycan layer of the lipoprotein. Digestion of the cleaved signal peptide also takes place upon cleavage of the signal peptide. In this review these chemical and topographical events are discussed step by step especially in relation to the process of protein secretion across the cytoplasmic membrane.Keywords
This publication has 48 references indexed in Scilit:
- Cloning and expression of a gene coding for the prolipoprotein signal peptidase of Escherichia coliFEBS Letters, 1983
- A temperature-sensitive mutant of E. coli exhibiting slow processing of exported proteinsCell, 1983
- Different exported proteins in E. coli show differences in the temporal mode of processing in vivoCell, 1981
- Interaction between Major Outer Membrane Protein (O‐8) and Lipopolysaccharide in Escherichia coli K12European Journal of Biochemistry, 1980
- Nature of the regions involved in the insertion of newly synthesized protein into the outer membrane of Escherichia coliBiochimica et Biophysica Acta (BBA) - Biomembranes, 1979
- The double helix coiled coil structure of murein lipoprotein from Escherichia coliJournal of Molecular Biology, 1978
- Covalent lipoprotein from the outer membrane of escherichia coliBiochimica et Biophysica Acta (BBA) - Reviews on Biomembranes, 1975
- Outer membrane proteins of Eschrichia coli: Biosynthesis and assemblyFEBS Letters, 1974
- In vivo biosynthesis on murein—lipoprotein of the outer membrane of E. coliFEBS Letters, 1973
- Areas of Adhesion between Wall and Membrane of Escherichia coliJournal of General Microbiology, 1968