This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Supplemental material
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Siméone, R.
Right arrow Articles by Chalut, C.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Siméone, R.
Right arrow Articles by Chalut, C.

 Previous Article  |  Next Article 

Journal of Bacteriology, July 2007, p. 4597-4602, Vol. 189, No. 13
0021-9193/07/$08.00+0     doi:10.1128/JB.00169-07
Copyright © 2007, American Society for Microbiology. All Rights Reserved.

Identification of the Missing trans-Acting Enoyl Reductase Required for Phthiocerol Dimycocerosate and Phenolglycolipid Biosynthesis in Mycobacterium tuberculosis{triangledown} ,{dagger}

Roxane Siméone, Patricia Constant, Christophe Guilhot, Mamadou Daffé, and Christian Chalut*

Département Mécanismes Moléculaires des Infections Mycobactériennes, Institut de Pharmacologie et de Biologie Structurale, UMR 5089 du CNRS et de l'Université Paul Sabatier, Toulouse, France

Received 1 February 2007/ Accepted 20 April 2007

Phthiocerol dimycocerosates (DIM) and phenolglycolipids (PGL) are functionally important surface-exposed lipids of Mycobacterium tuberculosis. Their biosynthesis involves the products of several genes clustered in a 70-kb region of the M. tuberculosis chromosome. Among these products is PpsD, one of the modular type I polyketide synthases responsible for the synthesis of the lipid core common to DIM and PGL. Bioinformatic analyses have suggested that this protein lacks a functional enoyl reductase activity domain required for the synthesis of these lipids. We have identified a gene, Rv2953, that putatively encodes an enoyl reductase. Mutation in Rv2953 prevents conventional DIM formation and leads to the accumulation of a novel DIM-like product. This product is unsaturated between C-4 and C-5 of phthiocerol. Consistently, complementation of the mutant with a functional pks15/1 gene from Mycobacterium bovis BCG resulted in the accumulation of an unsaturated PGL-like substance. When an intact Rv2953 gene was reintroduced into the mutant strain, the phenotype reverted to the wild type. These findings indicate that Rv2953 encodes a trans-acting enoyl reductase that acts with PpsD in phthiocerol and phenolphthiocerol biosynthesis.

* Corresponding author. Mailing address: Institut de Pharmacologie et Biologie Structurale, CNRS, 205 route de Narbonne, 31077 Toulouse Cedex, France. Phone: 33-5-61175473. Fax: 33-5-61175994. E-mail: christian.chalut{at}ipbs.fr

{triangledown} Published ahead of print on 27 April 2007.

{dagger} Supplemental material for this article may be found at http://jb.asm.org/.

Journal of Bacteriology, July 2007, p. 4597-4602, Vol. 189, No. 13
0021-9193/07/$08.00+0     doi:10.1128/JB.00169-07
Copyright © 2007, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Erb, T. J., Brecht, V., Fuchs, G., Muller, M., Alber, B. E. (2009). Carboxylation mechanism and stereochemistry of crotonyl-CoA carboxylase/reductase, a carboxylating enoyl-thioester reductase. Proc. Natl. Acad. Sci. USA 106: 8871-8876 [Abstract] [Full Text]  


Copyright © 2009 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»