2.50
Hdl Handle:
http://hdl.handle.net/10033/139960
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:
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.
Affiliation:
Institute for Biotechnology and Biomedicine, Universitat Autònoma de Barcelona, Bellaterra, 08193 Barcelona, Spain.
Citation:
Side effects of chaperone gene co-expression in recombinant protein production. 2010, 9:64 Microb. Cell Fact.
Journal:
Microbial cell factories
Issue Date:
2010
URI:
http://hdl.handle.net/10033/139960
DOI:
10.1186/1475-2859-9-64
PubMed ID:
20813055
Type:
Article
Language:
en
ISSN:
1475-2859
Appears in Collections:
publications of the research group recombinant protein expression (RPEX)

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.accessioned2011-08-17T13:35:58Z-
dc.date.available2011-08-17T13:35:58Z-
dc.date.issued2010-
dc.identifier.citationSide effects of chaperone gene co-expression in recombinant protein production. 2010, 9:64 Microb. Cell Fact.en
dc.identifier.issn1475-2859-
dc.identifier.pmid20813055-
dc.identifier.doi10.1186/1475-2859-9-64-
dc.identifier.urihttp://hdl.handle.net/10033/139960-
dc.description.abstractInsufficient 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.language.isoenen
dc.subject.meshBacterial Proteinsen
dc.subject.meshChaperonin 60en
dc.subject.meshEscherichia coli Proteinsen
dc.subject.meshHSP70 Heat-Shock Proteinsen
dc.subject.meshMolecular Chaperonesen
dc.subject.meshProtein Foldingen
dc.subject.meshProtein Stabilityen
dc.subject.meshRecombinant Proteinsen
dc.titleSide effects of chaperone gene co-expression in recombinant protein production.en
dc.typeArticleen
dc.contributor.departmentInstitute for Biotechnology and Biomedicine, Universitat Autònoma de Barcelona, Bellaterra, 08193 Barcelona, Spain.en
dc.identifier.journalMicrobial cell factoriesen
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