Details
| Original language | English |
|---|---|
| Pages (from-to) | 35-45 |
| Number of pages | 11 |
| Journal | Applied Microbiology and Biotechnology |
| Volume | 76 |
| Issue number | 1 |
| Publication status | Published - Aug 2007 |
| Externally published | Yes |
Abstract
The biotechnological production of recombinant proteins is challenged by processes that decrease the yield, such as protease action, aggregation, or misfolding. Today, the variation of strains and vector systems or the modulation of inducible promoter activities is commonly used to optimize expression systems. Alternatively, aggregation to inclusion bodies may be a desired starting point for protein isolation and refolding. The discovery of the twin-arginine translocation (Tat) system for folded proteins now opens new perspectives because in most cases, the Tat machinery does not allow the passage of unfolded proteins. This feature of the Tat system can be exploited for biotechnological purposes, as expression systems may be developed that ensure a virtually complete folding of a recombinant protein before purification. This review focuses on the characteristics that make recombinant Tat systems attractive for biotechnology and discusses problems and possible solutions for an efficient translocation of folded proteins.
Keywords
- Chaperones, Protein production, Protein secretion, PspA, Tat translocons, Twin-arginine translocation
ASJC Scopus subject areas
- Biochemistry, Genetics and Molecular Biology(all)
- Biotechnology
- Immunology and Microbiology(all)
- Applied Microbiology and Biotechnology
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In: Applied Microbiology and Biotechnology, Vol. 76, No. 1, 08.2007, p. 35-45.
Research output: Contribution to journal › Survey paper › Research › peer review
}
TY - JOUR
T1 - The twin-arginine translocation system and its capability for protein secretion in biotechnological protein production
AU - Brüser, Thomas
N1 - Funding Information: Acknowledgments I thank Jan R. Andreesen for the support and all the current and former members of my group for their efforts. Support by the Deutsche Forschungsgemeinschaft (grants BR 2285/1-3 and BR 2285/2-2) is gratefully acknowledged. Copyright: Copyright 2008 Elsevier B.V., All rights reserved.
PY - 2007/8
Y1 - 2007/8
N2 - The biotechnological production of recombinant proteins is challenged by processes that decrease the yield, such as protease action, aggregation, or misfolding. Today, the variation of strains and vector systems or the modulation of inducible promoter activities is commonly used to optimize expression systems. Alternatively, aggregation to inclusion bodies may be a desired starting point for protein isolation and refolding. The discovery of the twin-arginine translocation (Tat) system for folded proteins now opens new perspectives because in most cases, the Tat machinery does not allow the passage of unfolded proteins. This feature of the Tat system can be exploited for biotechnological purposes, as expression systems may be developed that ensure a virtually complete folding of a recombinant protein before purification. This review focuses on the characteristics that make recombinant Tat systems attractive for biotechnology and discusses problems and possible solutions for an efficient translocation of folded proteins.
AB - The biotechnological production of recombinant proteins is challenged by processes that decrease the yield, such as protease action, aggregation, or misfolding. Today, the variation of strains and vector systems or the modulation of inducible promoter activities is commonly used to optimize expression systems. Alternatively, aggregation to inclusion bodies may be a desired starting point for protein isolation and refolding. The discovery of the twin-arginine translocation (Tat) system for folded proteins now opens new perspectives because in most cases, the Tat machinery does not allow the passage of unfolded proteins. This feature of the Tat system can be exploited for biotechnological purposes, as expression systems may be developed that ensure a virtually complete folding of a recombinant protein before purification. This review focuses on the characteristics that make recombinant Tat systems attractive for biotechnology and discusses problems and possible solutions for an efficient translocation of folded proteins.
KW - Chaperones
KW - Protein production
KW - Protein secretion
KW - PspA
KW - Tat translocons
KW - Twin-arginine translocation
UR - http://www.scopus.com/inward/record.url?scp=34547569679&partnerID=8YFLogxK
U2 - 10.1007/s00253-007-0991-z
DO - 10.1007/s00253-007-0991-z
M3 - Survey paper
C2 - 17476499
AN - SCOPUS:34547569679
VL - 76
SP - 35
EP - 45
JO - Applied Microbiology and Biotechnology
JF - Applied Microbiology and Biotechnology
SN - 0175-7598
IS - 1
ER -