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Export and secretion of overproduced OmpA‐β‐lactamase in Escherichia coli
Author(s) -
Bolla Jean-Michel,
Lazdunski Claude,
Inouye Masayori,
Pagès Jean-Marie
Publication year - 1987
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(87)80450-7
Subject(s) - periplasmic space , signal peptide , escherichia coli , secretion , cleavage (geology) , peptide , chemistry , cloning (programming) , overproduction , biochemistry , biology , peptide sequence , gene , computer science , paleontology , fracture (geology) , programming language
The export of β‐lactamase to the periplasm of Escherichia coli can be directed by the OmpA signal peptide in the secretion cloning vector pIN‐III. The overproduction of the hybrid precursor specifically induces a delay in the onset of processing of newly synthesized polypeptide chains. However, when the processing starts, no alteration in the rate of cleavage itself is observed. Our results suggest that the temporal mode of processing (which reflects translocation) does not depend on the nature of the signal peptide but rather depends on the nature of the polypeptide chain exported.