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J. Biol. Chem., Vol. 279, Issue 28, 28835-28843, July 9, 2004

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Trehalose Is Required for Growth of Mycobacterium smegmatis^*

Peter J. Woodruff, Brian L. Carlson, Bunpote Siridechadilok, Matthew R. Pratt¶, Ryan H. Senaratne, Joseph D. Mougous, Lee W. Riley, Spencer J. Williams¶||, and Carolyn R. Bertozzi¶**

From the Departments of ^¶Chemistry and Molecular and Cell Biology and School of Public Health and ^**Howard Hughes Medical Institute, University of California, Berkeley, California 94720

Mycobacteria contain high levels of the disaccharide trehalose in free form as well as within various immunologically relevant glycolipids such as cord factor and sulfolipid-1. By contrast, most bacteria use trehalose solely as a general osmoprotectant or thermoprotectant. Mycobacterium tuberculosis and Mycobacterium smegmatis possess three pathways for the synthesis of trehalose. Most bacteria possess only one trehalose biosynthesis pathway and do not elaborate the disaccharide into more complex metabolites, suggesting a distinct role for trehalose in mycobacteria. We disabled key enzymes required for each of the three pathways in M. smegmatis by allelic replacement. The resulting trehalose biosynthesis mutant was unable to proliferate and enter stationary phase unless supplemented with trehalose. At elevated temperatures, however, the mutant was unable to proliferate even in the presence of trehalose. Genetic complementation experiments showed that each of the three pathways was able to recover the mutant in the absence of trehalose, even at elevated temperatures. From a panel of trehalose analogs, only those with the native ,-(1,1) anomeric stereochemistry rescued the mutant, whereas alternate stereoisomers and general osmo- and thermoprotectants were inactive. These findings suggest a dual role for trehalose as both a thermoprotectant and a precursor of critical cell wall metabolites.

Received for publication, December 2, 2003 , and in revised form, April 19, 2004.

^* This work was supported by National Institutes of Health Grant AI51622 (to C. R. B.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The on-line version of this article (available at http://www.jbc.org) contains supplemental Fig. S1).

Received a predoctoral fellowship from the National Science Foundation.

^|| Howard Hughes Medical Institute Fellow of the Life Sciences Research Foundation. To whom correspondence may be addressed. Present address: School of Chemistry, University of Melbourne, Parkville, Victoria, Australia 3054. E-mail: sjwill{at}unimelb.edu.au. To whom correspondence may be addressed. E-mail: crb{at}berkeley.edu.

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