Maturation of Escherichia coli maltose-binding protein by signal peptidase I in vivo. Sequence requirements for efficient processing and demonstration of an alternate cleavage site.
Open Access
- 1 February 1990
- journal article
- research article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 265 (6) , 3417-3423
- https://doi.org/10.1016/s0021-9258(19)39783-2
Abstract
No abstract availableThis publication has 40 references indexed in Scilit:
- Protein Translocation Across MembranesScience, 1988
- The antifolding activity of SecB promotes the export of the E. coli maltose-binding proteinCell, 1988
- Purification and characterization of hen oviduct microsomal signal peptidaseBiochemistry, 1987
- Signal sequencesJournal of Molecular Biology, 1985
- Patterns of Amino Acids near Signal‐Sequence Cleavage SitesEuropean Journal of Biochemistry, 1983
- A putative signal peptidase recognition site and sequence in eukaryotic and prokaryotic signal peptidesJournal of Molecular Biology, 1983
- Diverse effects of mutations in the signal sequence on the secretion of β-lactamase in Salmonella typhimuriumCell, 1982
- Processing of filamentous phage pre-coat proteinJournal of Molecular Biology, 1980
- Secretion and Membrane Localization of Proteins inEscherichia ColiCritical Reviews in Biochemistry, 1980
- Affinity chromatographic isolation of the periplasmic maltose binding protein of Escherichia coliFEBS Letters, 1978