NDLI: Structural analysis of substrate binding by the TatBC component of the twin-arginine protein transport system

Content Provider	PubMed Central
Author	Tarry, Michael J. Schäfer, Eva Chen, Shuyun Buchanan, Grant Greene, Nicholas P. Lea, Susan M. Palmer, Tracy Saibil, Helen R. Berks, Ben C.
Abstract	The Tat system transports folded proteins across the bacterial cytoplasmic membrane and the thylakoid membrane of plant chloroplasts. In Escherichia coli substrate proteins initially bind to the integral membrane TatBC complex which then recruits the protein TatA to effect translocation. Overproduction of TatBC and the substrate protein SufI in the absence of TatA led to the accumulation of TatBC-SufI complexes that could be purified using an affinity tag on the substrate. Three-dimensional structures of the TatBC-SufI complexes and unliganded TatBC were obtained by single-particle electron microscopy and random conical tilt reconstruction. Comparison of the structures shows that substrate molecules bind on the periphery of the TatBC complex and that substrate binding causes a significant reduction in diameter of the TatBC part of the complex. Although the TatBC complex contains multiple copies of the signal peptide-binding TatC protomer, purified TatBC-SufI complexes contain only 1 or 2 SufI molecules. Where 2 substrates are present in the TatBC-SufI complex, they are bound at adjacent sites. These observations imply that only certain TatC protomers within the complex interact with substrate or that there is a negative cooperativity of substrate binding. Similar TatBC-substrate complexes can be generated by an alternative in vitro reconstitution method and using a different substrate protein.
Related Links	http://dx.doi.org/10.1073/pnas.0901566106
Ending Page	13289
Page Count	6
Starting Page	13284
File Format	PDF
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	32
Volume Number	106
Language	English
Publisher	National Academy of Sciences
Publisher Date	2009-08-11
Access Restriction	Open
Rights Holder	National Academy of Sciences
Subject Keyword	General Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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Structural model for the protein-translocating element of the twin-arginine transport system

Live cell imaging shows reversible assembly of the TatA component of the twin-arginine protein transport system

The early mature part of bacterial twin-arginine translocation (Tat) precursor proteins contributes to TatBC receptor binding

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The TatA component of the twin-arginine protein transport system forms channel complexes of variable diameter

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Structural diversity in twin-arginine signal peptide-binding proteins.

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Structural analysis of substrate binding by the TatBC component of the twin-arginine protein transport system

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