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J. Bacteriol. doi:10.1128/JB.01740-06
Copyright (c) 2007, American Society for Microbiology and/or the Listed Authors/Institutions. All Rights Reserved.

Functional complementation of the essential gene fabG1 of Mycobacterium tuberculosis by Mycobacterium smegmatis fabG, but not Escherichia coli fabG

Centre for Infectious Disease, Institute of Cell and Molecular Science, Barts and the London, London, E1 2AT, UK; Institut de Pharmacologie et Biologie Structurale (UMR5089), Department of Molecular Mechanisms of Mycobacterial Infections, Centre National de la Recherche Scientifique and Université Paul Sabatier (Toulouse III), 205 Route de Narbonne, F-31077 Toulouse Cedex, France; GlaxoSmithKline, 1250 South Collegeville Road, Collegeville, PA 19426, USA; GlaxoSmithKline, Gunnels Wood Road, Stevenage, Hertfordshire, SG1 2NY, UK

^* To whom correspondence should be addressed. Email: t.parish{at}qmul.ac.uk.

	Abstract

Mycolic acids are a key component of the mycobacterial cell wall, providing structure and forming a major permeability barrier. In Mycobacterium tuberculosis mycolic acids are synthesised by type I and type II fatty acid synthases. One of the enzymes of the type II system is encoded by fabG1. We demonstrate that this gene can only be deleted from the M. tuberculosis chromosome when a second functional copy is provided elsewhere, showing that under normal culture conditions, fabG1 is essential. FabG1 activity can be replaced by the corresponding enzyme from the closely related species Mycobacterium smegmatis, but not by the enzyme from Escherichia coli. M. tuberculosis carrying FabG from M. smegmatis showed no phenotypic changes and both the mycolic acids and cell wall permeability were unchanged. Thus M. tuberculosis and M. smegmatis enzymes are interchangeable and do not control the length and types of mycolic acids synthesised.

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