Show simple item record

dc.contributor.authorMartínez-Alonso, Mónica
dc.contributor.authorGarcía-Fruitós, Elena
dc.contributor.authorFerrer-Miralles, Neus
dc.contributor.authorRinas, Ursula
dc.contributor.authorVillaverde, Antonio
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.
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
refterms.dateFOA2018-06-13T05:41:34Z
html.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.


Files in this item

Thumbnail
Name:
12934_2010_Article_454.pdf
Size:
463.7Kb
Format:
PDF

This item appears in the following Collection(s)

Show simple item record