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J. Biol. Chem., Vol. 277, Issue 12, 10362-10366, March 22, 2002

This Article Full Text Full Text (PDF) All Versions of this Article: 277/12/10362    most recent M109135200v1 Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Allen, S. C. H. Articles by Robinson, C. Search for Related Content PubMed PubMed Citation Articles by Allen, S. C. H. Articles by Robinson, C. Social Bookmarking                      What's this?

Essential Cytoplasmic Domains in the Escherichia coli TatC Protein^*

Stuart C. H. Allen, Claire M. L. Barrett, Nicola Ray, and Colin Robinson

From the Department of Biological Sciences, University of Warwick, Coventry CV4 7AL, United Kingdom

The twin-arginine translocation (Tat) system mediates the transport of proteins across the bacterial plasma membrane and chloroplast thylakoid membrane. Operating in parallel with Sec-type systems in these membranes, the Tat system is completely different in both structural and mechanistic terms, and is uniquely able to catalyze the translocation of fully folded proteins across coupled membranes. TatC is an essential, multispanning component that has been proposed to form part of the binding site for substrate precursor proteins. In this study we have tested the importance of conserved residues on the periplasmic and cytoplasmic face of the Escherichia coli protein. We find that many of the mutations on the cytoplasmic face have little or no effect. However, substitution at several positions in the extreme N-terminal cytoplasmic region or the predicted first cytoplasmic loop lead to a significant or complete loss of Tat-dependent export. The mutated strains are unable to grow anaerobically on trimethylamine N-oxide minimal media and are unable to export trimethylamine-N-oxide reductase (TorA). The same mutants are completely unable to export a chimeric protein, comprising the TorA signal peptide linked to green fluorescent protein, indicating that translocation is blocked rather than cofactor insertion into the TorA mature protein. The data point to two essential cytoplasmic domains on the TatC protein that are essential for export.

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