Details
| Originalsprache | Englisch |
|---|---|
| Aufsatznummer | 64 |
| Fachzeitschrift | Microbial cell factories |
| Jahrgang | 9 |
| Publikationsstatus | Veröffentlicht - 2 Sept. 2010 |
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.
ASJC Scopus Sachgebiete
- Biochemie, Genetik und Molekularbiologie (insg.)
- Biotechnologie
- Chemische Verfahrenstechnik (insg.)
- Bioengineering
- Immunologie und Mikrobiologie (insg.)
- Angewandte Mikrobiologie und Biotechnologie
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in: Microbial cell factories, Jahrgang 9, 64, 02.09.2010.
Publikation: Beitrag in Fachzeitschrift › Artikel › Forschung › Peer-Review
}
TY - JOUR
T1 - Side effects of chaperone gene co-expression in recombinant protein production
AU - Martínez-Alonso, Mónica
AU - García-Fruitós, Elena
AU - Ferrer-Miralles, Neus
AU - Rinas, Ursula
AU - Villaverde, Antonio
N1 - Funding Information: The authors appreciate the financial support through MEC (BIO2007-61194). We also appreciate the support from The Biomedical Research Networking Center in Bioengineering, Biomaterials and Nanomedicine (CIBER-BBN, Spain), an initiative funded by the VI National R&D&i Plan 2008-2011, Iniciativa Ingenio 2010, Consolider Program, CIBER Actions and financed by the Instituto de Salud Carlos III with assistance from the European Regional Development Fund. Antonio Villaverde has been granted with an ICREA ACADEMIA award (from ICREA, Catalonia, Spain).
PY - 2010/9/2
Y1 - 2010/9/2
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=77956457332&partnerID=8YFLogxK
U2 - 10.1186/1475-2859-9-64
DO - 10.1186/1475-2859-9-64
M3 - Article
C2 - 20813055
AN - SCOPUS:77956457332
VL - 9
JO - Microbial cell factories
JF - Microbial cell factories
SN - 1475-2859
M1 - 64
ER -