Transport of Folded Proteins by the Tat System
Autor: | Kelly M. Frain, Colin Robinson, Jan Maarten van Dijl |
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Rok vydání: | 2019 |
Předmět: |
Signal peptide
Protein Folding Twin-Arginine-Translocation System/chemistry Protein Sorting Signals/physiology Arginine/physiology Bioengineering Bacillus subtilis Protein Sorting Signals Twin-arginine Arginine Biochemistry Article Analytical Chemistry Protein Transport/physiology Twin-arginine translocation pathway Membrane Transport Proteins/chemistry Escherichia coli TatA SEC Translocation Channels/chemistry TatC Electrochemical gradient TatB Twin-Arginine-Translocation System biology Chemistry Escherichia coli Proteins Cell Membrane/metabolism Cell Membrane Organic Chemistry Membrane Transport Proteins Biological membrane biology.organism_classification Cell biology Transport protein Protein Transport Cytoplasm Escherichia coli Proteins/chemistry Proofreading SEC Translocation Channels |
Zdroj: | The Protein Journal |
ISSN: | 1875-8355 1572-3887 |
Popis: | The twin-arginine protein translocation (Tat) system has been characterized in bacteria, archaea and the chloroplast thylakoidal membrane. This system is distinct from other protein transport systems with respect to two key features. Firstly, it accepts cargo proteins with an N-terminal signal peptide that carries the canonical twin-arginine motif, which is essential for transport. Second, the Tat system only accepts and translocates fully folded cargo proteins across the respective membrane. Here, we review the core essential features of folded protein transport via the bacterial Tat system, using the three-component TatABC system of Escherichia coli and the two-component TatAC systems of Bacillus subtilis as the main examples. In particular, we address features of twin-arginine signal peptides, the essential Tat components and how they assemble into different complexes, mechanistic features and energetics of Tat-dependent protein translocation, cytoplasmic chaperoning of Tat cargo proteins, and the remarkable proofreading capabilities of the Tat system. In doing so, we present the current state of our understanding of Tat-dependent protein translocation across biological membranes, which may serve as a lead for future investigations. |
Databáze: | OpenAIRE |
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