2.50
Hdl Handle:
http://hdl.handle.net/10033/620788
Title:
Side effects of chaperone gene co-expression in recombinant protein production
Authors:
Martínez-Alonso, Mónica; García-Fruitós, Elena; Ferrer-Miralles, Neus; Rinas, Ursula; Villaverde, Antonio
Abstract:
Abstract Insufficient availability of molecular chaperones is observed as a major bottleneck for proper protein folding in recombinant protein production. Therefore, co-production of selected sets of cell chaperones along with foreign polypeptides is a common approach to increase the yield of properly folded, recombinant proteins in bacterial cell factories. However, unbalanced amounts of folding modulators handling folding-reluctant protein species might instead trigger undesired proteolytic activities, detrimental regarding recombinant protein stability, quality and yield. This minireview summarizes the most recent observations of chaperone-linked negative side effects, mostly focusing on DnaK and GroEL sets, when using these proteins as folding assistant agents. These events are discussed in the context of the complexity of the cell quality network and the consequent intricacy of the physiological responses triggered by protein misfolding.
Citation:
Microbial Cell Factories. 2010 Sep 02;9(1):64
Issue Date:
2-Sep-2010
URI:
http://dx.doi.org/10.1186/1475-2859-9-64; http://hdl.handle.net/10033/620788
Type:
Journal Article
Appears in Collections:
Publications of the Dept. Structure and Functions of Proteins(SFPR)

Full metadata record

DC FieldValue Language
dc.contributor.authorMartínez-Alonso, Mónicaen
dc.contributor.authorGarcía-Fruitós, Elenaen
dc.contributor.authorFerrer-Miralles, Neusen
dc.contributor.authorRinas, Ursulaen
dc.contributor.authorVillaverde, Antonioen
dc.date.accessioned2017-01-27T11:49:56Z-
dc.date.available2017-01-27T11:49:56Z-
dc.date.issued2010-09-02en
dc.identifier.citationMicrobial Cell Factories. 2010 Sep 02;9(1):64en
dc.identifier.urihttp://dx.doi.org/10.1186/1475-2859-9-64en
dc.identifier.urihttp://hdl.handle.net/10033/620788-
dc.description.abstractAbstract Insufficient availability of molecular chaperones is observed as a major bottleneck for proper protein folding in recombinant protein production. Therefore, co-production of selected sets of cell chaperones along with foreign polypeptides is a common approach to increase the yield of properly folded, recombinant proteins in bacterial cell factories. However, unbalanced amounts of folding modulators handling folding-reluctant protein species might instead trigger undesired proteolytic activities, detrimental regarding recombinant protein stability, quality and yield. This minireview summarizes the most recent observations of chaperone-linked negative side effects, mostly focusing on DnaK and GroEL sets, when using these proteins as folding assistant agents. These events are discussed in the context of the complexity of the cell quality network and the consequent intricacy of the physiological responses triggered by protein misfolding.en
dc.titleSide effects of chaperone gene co-expression in recombinant protein productionen
dc.typeJournal Articleen
dc.language.rfc3066enen
dc.rights.holderMartínez-Alonso et al.en
dc.date.updated2015-09-04T08:26:01Zen
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