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Appl. Environ. Microbiol. doi:10.1128/AEM.01528-06
Copyright (c) 2006, American Society for Microbiology and/or the Listed Authors/Institutions. All Rights Reserved.

Functional Analysis of the Twin-Arginine Translocation Pathway in Corynebacterium glutamicum ATCC13869

Institute of Life Sciences, Ajinomoto Co., Inc., Kawasaki 210-8681, Japan, and Laboratoire de Chimie Bactérienne, UPR9043, Institut de Biologie Structurale et Microbiologie, CNRS, F-13402 Marseille, France

	Abstract

Compared to other Gram positive bacteria, the genetic structure of Corynebacterium glutamicum Tat system is unique in that it contains the tatE gene in addition to tatA, tatB, and tatC. The tatE homologue has been detected only in the genomes of Gram negative enterobacteria. To assess the function of the C. glutamicum Tat pathway, we cloned the tatA, tatB, tatC, and tatE genes from C. glutamicum ATCC13869 and constructed mutants carrying deletions of each tat gene or both the tatA and the tatE genes. Using the green fluorescent protein fused with the twin-arginine signal peptide of E. coli TorA protein we demonstrated that the minimal functional Tat system required TatA and TatC. TatA and TatE provide overlapping fuction. Unlike the TatB proteins from Gram negative bacteria, C. glutamicum TatB was dispensable for the Tat function, although it was required for the maximal efficiency of the secretion. The signal peptide sequence of the isomalto-dextranase (IMD) of Arthrobacter globiformis contains a twin-arginine motif. We showed that both IMD and GFP fused with the signal peptide of IMD were secreted via the C. glutamicum Tat pathway. These observations indicated that IMD is a bona fide Tat substrate and implies a great potential of the C. glutamicum Tat system in industrial production of heterologous folded proteins.