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Recolector de Ciencia Abierta, RECOLECTA
Article . 1996
License: CC BY NC SA
Data sources: Recolector de Ciencia Abierta, RECOLECTA
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Recolector de Ciencia Abierta, RECOLECTA
Article . 1996
License: CC BY NC SA
Data sources: Recolector de Ciencia Abierta, RECOLECTA
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Recolector de Ciencia Abierta, RECOLECTA
Article . 2023
Data sources: Recolector de Ciencia Abierta, RECOLECTA
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Claim

Different Pr1A proteins increase the efficiency of periplasmic production of human interleukin-6 in Escherichia coli

descriptionPublicationkeyboard_double_arrow_right Article 01 Jan 1996 English Publisher:Elsevier BV
Authors: Pérez-Pérez, J.; Barbero, J. L.; Márquez, G.; Gutiérrez, J.;

handle: 10261/294350

Different Pr1A proteins increase the efficiency of periplasmic production of human interleukin-6 in Escherichia coli

Abstract

The export efficiency of a fusion of the Escherichia coli preOmpA signal peptide to human interleukin-6 can be significantly raised by coexpressing three different prlA alleles of secY along with wild type secE. The effect seems prlA-specific, as prlG1 (a prl allele of secE) does not affect the export of preOmpA-hIL-6. Coexpression of secD and secF also stimulates the export of the fusion protein. The export efficiency of a fusion of the Escherichia coli preOmpA signal peptide to human interleukin-6 can be significantly raised by coexpressing three different prlA alleles of secY along with wild type secE. The effect seems prlA-specific, as prlG1 (a prl allele of secE) does not affect the export of preOmpA-hIL-6. Coexpression of secD and secF also stimulates the export of the fusion protein.

Keywords

set Y, Interleukin-6, Protein secretion

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popularity
This indicator reflects the "current" impact/attention (the "hype") of an article in the research community at large, based on the underlying citation network.
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This indicator reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).
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