NDLI: Following the path of a twin-arginine precursor along the TatABC translocase of Escherichia coli.

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Following the path of a twin-arginine precursor along the TatABC translocase of Escherichia coli.

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Following the path of a twin-arginine precursor along the TatABC translocase of Escherichia coli.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Delisa, Matthew P. Müller, Matthias Panahandeh, Sascha Maurer, Carlo Moser, Michael
Description	Author Affiliation: Panahandeh S ( Institut für Biochemie und Molekularbiologie, ZBMZ, Freiburg, Germany.)
Abstract	The twin-arginine translocation (Tat) machinery present in bacterial and thylakoidal membranes is able to transport fully folded proteins. Consistent with previous in vivo data, we show that the model Tat substrate TorA-PhoA is translocated by the TatABC translocase of Escherichia coli inner membrane vesicles, only if the PhoA moiety was allowed to fold by disulfide bond formation. Although even unfolded TorA-PhoA was found to physically associate with the Tat translocase of the vesicles, site-specific cross-linking revealed a perturbed interaction of the signal sequence of unfolded TorA-PhoA with the TatBC receptor site. Some of the folded TorA-PhoA precursor accumulated in a partially protease-protected membrane environment, from where it could be translocated into the lumen of the vesicles upon re-installation of an H+-gradient. Translocation arrest occurred in immediate vicinity to TatA. Consistent with a neighborhood to TatA, TorA-PhoA remained protease-resistant in the presence of detergents that are known to preserve the oligomeric structures of TatA. Moreover, entry of TorA-PhoA to the protease-protected environment strictly required the presence of TatA. Collectively, our results are consistent with some degree of quality control by TatBC and a recruitment of TatA to a folded substrate that has functionally engaged the twin-arginine translocase.
ISSN	00219258
e-ISSN	1083351X
Journal	Journal of Biological Chemistry
Issue Number	48
Volume Number	283
Language	English
Publisher	American Society for Biochemistry and Molecular Biology (United States)
Publisher Date	2008-11-28
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Alkaline Phosphatase Metabolism Cell Membrane Enzymology Escherichia Coli Proteins Escherichia Coli Membrane Transport Proteins Oxidoreductases, N-Demethylating Protein Folding Genetics Chemistry Protein Transport Physiology Research Support, Non-U.S. Gov't Biochemistry Molecular Biology
Content Type	Text
Resource Type	Article
Subject	Cell Biology Biochemistry Molecular Biology

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