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The twin-arginine translocation system and its capability for protein secretion in biotechnological protein production

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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.

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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.

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  1. Institute of Biology, Division of Microbiology, Martin-Luther-University Halle-Wittenberg, Kurt-Mothes-Str. 3, 06120, Halle, Germany

    Thomas Brüser

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Brüser, T. The twin-arginine translocation system and its capability for protein secretion in biotechnological protein production. Appl Microbiol Biotechnol 76, 35–45 (2007). https://doi.org/10.1007/s00253-007-0991-z

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