The twin-arginine translocation system and its capability for protein secretion in biotechnological protein production.
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.
Brüser
Thomas
T
Institute of Biology, Division of Microbiology, Martin-Luther-University Halle-Wittenberg, Kurt-Mothes-Str. 3, 06120, Halle, Germany. t.brueser@mikrobiologie.uni-halle.de
D029968:Escherichia coli Proteins; D026901:Membrane Transport Proteins / Q000502:physiology*; D015202:Protein Engineering; D017510:Protein Folding; D021381:Protein Transport; D011994:Recombinant Proteins / Q000096:biosynthesis / Q000378:metabolism
D029968:Escherichia coli Proteins; D026901:Membrane Transport Proteins; D011994:Recombinant Proteins; C408585:twin-arginine translocase complex, E coli