Export and secretion of overproduced OmpA-β-lactamase in Escherichia coli

Jean Michel Bolla; Claude Lazdunski; Masayori Inouye; Jean Marie Pagès

doi:10.1016/0014-5793(87)80450-7

Export and secretion of overproduced OmpA-β-lactamase in Escherichia coli

Jean Michel Bolla, Claude Lazdunski, Masayori Inouye, Jean Marie Pagès

Research output: Contribution to journal › Article › peer-review

12 Scopus citations

Abstract

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.

Original language	English (US)
Pages (from-to)	213-218
Number of pages	6
Journal	FEBS Letters
Volume	224
Issue number	1
DOIs	https://doi.org/10.1016/0014-5793(87)80450-7
State	Published - Nov 16 1987

All Science Journal Classification (ASJC) codes

Biophysics
Structural Biology
Biochemistry
Molecular Biology
Genetics
Cell Biology

Keywords

Hybrid protein
Periplasmic protein
Protein export
Protein processing
Signal peptide

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10.1016/0014-5793(87)80450-7

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title = "Export and secretion of overproduced OmpA-β-lactamase in Escherichia coli",

abstract = "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.",

keywords = "Hybrid protein, Periplasmic protein, Protein export, Protein processing, Signal peptide",

author = "Bolla, {Jean Michel} and Claude Lazdunski and Masayori Inouye and Pag{\`e}s, {Jean Marie}",

note = "Funding Information: We thank S.P. Howard for careful reading and M. Payan for preparing the manuscript. We thank Drs G. Ferro-Luzzi Ames and G. Cesarini, and Im-munotech for the generous gift of antisera. This work was supported by the Centre National de la Recherche Scientifique, the Institut National de la Sant~ et de la Recherche M6dicale, the Fondation pour la Recherche M6dicale.",

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doi = "10.1016/0014-5793(87)80450-7",

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T1 - Export and secretion of overproduced OmpA-β-lactamase in Escherichia coli

AU - Bolla, Jean Michel

AU - Lazdunski, Claude

AU - Inouye, Masayori

AU - Pagès, Jean Marie

N1 - Funding Information: We thank S.P. Howard for careful reading and M. Payan for preparing the manuscript. We thank Drs G. Ferro-Luzzi Ames and G. Cesarini, and Im-munotech for the generous gift of antisera. This work was supported by the Centre National de la Recherche Scientifique, the Institut National de la Sant~ et de la Recherche M6dicale, the Fondation pour la Recherche M6dicale.

PY - 1987/11/16

Y1 - 1987/11/16

N2 - 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.

AB - 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.

KW - Hybrid protein

KW - Periplasmic protein

KW - Protein export

KW - Protein processing

KW - Signal peptide

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DO - 10.1016/0014-5793(87)80450-7

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JO - FEBS Letters

JF - FEBS Letters

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ER -

Export and secretion of overproduced OmpA-β-lactamase in Escherichia coli

Abstract

All Science Journal Classification (ASJC) codes

Keywords

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