DisCoTune: versatile auxiliary plasmids for the production of disulphide‐containing proteins and peptides in the E. coli T7 system

Summary Secreted proteins and peptides hold large potential both as therapeutics and as enzyme catalysts in biotechnology. The high stability of many secreted proteins helps maintain functional integrity in changing chemical environments and is a contributing factor to their commercial potential. Di...

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Autores principales:	Andreas B. Bertelsen, Celeste Menuet Hackney, Carolyn N. Bayer, Lau D. Kjelgaard, Maja Rennig, Brian Christensen, Esben Skipper Sørensen, Helena Safavi‐Hemami, Tune Wulff, Lars Ellgaard, Morten H. H. Nørholm
Formato:	article
Lenguaje:	EN
Publicado:	Wiley 2021
Materias:	Biotechnology TP248.13-248.65
Acceso en línea:	https://doaj.org/article/ae7d52884de74d71a1a0d3932c06a51c
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spelling	oai:doaj.org-article:ae7d52884de74d71a1a0d3932c06a51c2021-11-18T15:39:53ZDisCoTune: versatile auxiliary plasmids for the production of disulphide‐containing proteins and peptides in the E. coli T7 system1751-791510.1111/1751-7915.13895https://doaj.org/article/ae7d52884de74d71a1a0d3932c06a51c2021-11-01T00:00:00Zhttps://doi.org/10.1111/1751-7915.13895https://doaj.org/toc/1751-7915Summary Secreted proteins and peptides hold large potential both as therapeutics and as enzyme catalysts in biotechnology. The high stability of many secreted proteins helps maintain functional integrity in changing chemical environments and is a contributing factor to their commercial potential. Disulphide bonds constitute an important post‐translational modification that stabilizes many of these proteins and thus preserves the active state under chemically stressful conditions. Despite their importance, the discovery and applications within this group of proteins and peptides are limited by the availability of synthetic biology tools and heterologous production systems that allow for efficient formation of disulphide bonds. Here, we refine the design of two DisCoTune (Disulphide bond formation in E. coli with tunable expression) plasmids that enable the formation of disulphides in the highly popular Escherichia coli T7 protein production system. We show that this new system promotes significantly higher yield and activity of an industrial protease and a conotoxin, which belongs to a group of disulphide‐rich venom peptides from cone snails with strong potential as research tools and pharmacological agents.Andreas B. BertelsenCeleste Menuet HackneyCarolyn N. BayerLau D. KjelgaardMaja RennigBrian ChristensenEsben Skipper SørensenHelena Safavi‐HemamiTune WulffLars EllgaardMorten H. H. NørholmWileyarticleBiotechnologyTP248.13-248.65ENMicrobial Biotechnology, Vol 14, Iss 6, Pp 2566-2580 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Biotechnology TP248.13-248.65
spellingShingle	Biotechnology TP248.13-248.65 Andreas B. Bertelsen Celeste Menuet Hackney Carolyn N. Bayer Lau D. Kjelgaard Maja Rennig Brian Christensen Esben Skipper Sørensen Helena Safavi‐Hemami Tune Wulff Lars Ellgaard Morten H. H. Nørholm DisCoTune: versatile auxiliary plasmids for the production of disulphide‐containing proteins and peptides in the E. coli T7 system
description	Summary Secreted proteins and peptides hold large potential both as therapeutics and as enzyme catalysts in biotechnology. The high stability of many secreted proteins helps maintain functional integrity in changing chemical environments and is a contributing factor to their commercial potential. Disulphide bonds constitute an important post‐translational modification that stabilizes many of these proteins and thus preserves the active state under chemically stressful conditions. Despite their importance, the discovery and applications within this group of proteins and peptides are limited by the availability of synthetic biology tools and heterologous production systems that allow for efficient formation of disulphide bonds. Here, we refine the design of two DisCoTune (Disulphide bond formation in E. coli with tunable expression) plasmids that enable the formation of disulphides in the highly popular Escherichia coli T7 protein production system. We show that this new system promotes significantly higher yield and activity of an industrial protease and a conotoxin, which belongs to a group of disulphide‐rich venom peptides from cone snails with strong potential as research tools and pharmacological agents.
format	article
author	Andreas B. Bertelsen Celeste Menuet Hackney Carolyn N. Bayer Lau D. Kjelgaard Maja Rennig Brian Christensen Esben Skipper Sørensen Helena Safavi‐Hemami Tune Wulff Lars Ellgaard Morten H. H. Nørholm
author_facet	Andreas B. Bertelsen Celeste Menuet Hackney Carolyn N. Bayer Lau D. Kjelgaard Maja Rennig Brian Christensen Esben Skipper Sørensen Helena Safavi‐Hemami Tune Wulff Lars Ellgaard Morten H. H. Nørholm
author_sort	Andreas B. Bertelsen
title	DisCoTune: versatile auxiliary plasmids for the production of disulphide‐containing proteins and peptides in the E. coli T7 system
title_short	DisCoTune: versatile auxiliary plasmids for the production of disulphide‐containing proteins and peptides in the E. coli T7 system
title_full	DisCoTune: versatile auxiliary plasmids for the production of disulphide‐containing proteins and peptides in the E. coli T7 system
title_fullStr	DisCoTune: versatile auxiliary plasmids for the production of disulphide‐containing proteins and peptides in the E. coli T7 system
title_full_unstemmed	DisCoTune: versatile auxiliary plasmids for the production of disulphide‐containing proteins and peptides in the E. coli T7 system
title_sort	discotune: versatile auxiliary plasmids for the production of disulphide‐containing proteins and peptides in the e. coli t7 system
publisher	Wiley
publishDate	2021
url	https://doaj.org/article/ae7d52884de74d71a1a0d3932c06a51c
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DisCoTune: versatile auxiliary plasmids for the production of disulphide‐containing proteins and peptides in the E. coli T7 system

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