This Article
Right arrow Full Text
Right arrow Full Text (PDF)
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 Crick, D. C.
Right arrow Articles by Brennan, P. J.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Crick, D. C.
Right arrow Articles by Brennan, P. J.

 Previous Article  |  Next Article 

Journal of Bacteriology, October 2000, p. 5771-5778, Vol. 182, No. 20
0021-9193/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.

Polyprenyl Phosphate Biosynthesis in Mycobacterium tuberculosis and Mycobacterium smegmatis

Dean C. Crick,1,* Mark C. Schulbach,1 Erin E. Zink,1 Marco Macchia,2 Silvia Barontini,2 Gurdyal S. Besra,3 and Patrick J. Brennan1

Department of Microbiology, Colorado State University, Fort Collins, Colorado 80523-16771; Università di Pisa, Dipartimento di Scienze Farmaceutiche, 56126 Pisa, Italy2; and School of Microbiological, Immunological, and Virological Sciences, University of Newcastle upon Tyne, Newcastle upon Tyne, United Kingdom3

Received 22 May 2000/Accepted 25 July 2000

Mycobacterium smegmatis has been shown to contain two forms of polyprenyl phosphate (Pol-P), while Mycobacterium tuberculosis contains only one. Utilizing subcellular fractions from M. smegmatis and M. tuberculosis, we show that Pol-P synthesis is different in these species. The specific activities of the prenyl diphosphate synthases in M. tuberculosis are 10- to 100-fold lower than those in M. smegmatis. In M. smegmatis decaprenyl diphosphate and heptaprenyl diphosphate were the main products synthesized in vitro, whereas in M. tuberculosis only decaprenyl diphosphate was synthesized. The data from both organisms suggest that geranyl diphosphate is the allylic substrate for two distinct prenyl diphosphate synthases, one located in the cell membrane that synthesizes omega ,E,Z-farnesyl diphosphate and the other present in the cytosol that synthesizes omega ,E,E,E-geranylgeranyl diphosphate. In M. smegmatis, the omega ,E,Z-farnesyl diphosphate is utilized by a membrane-associated prenyl diphosphate synthase activity to generate decaprenyl diphosphate, and the omega ,E,E,E-geranylgeranyl diphosphate is utilized by a membrane-associated activity for the synthesis of the heptaprenyl diphosphate. In M. tuberculosis, however, omega ,E,E,E-geranylgeranyl diphosphate is not utilized for the synthesis of heptaprenyl diphosphate. Thus, the difference in the compositions of the Pol-P of M. smegmatis and M. tuberculosis can be attributed to distinct enzymatic differences between these two organisms.

* Corresponding author. Mailing address: Department of Microbiology, Colorado State University, Fort Collins, CO 80523-1677. Phone: (970) 491-3308. Fax: (970) 491-1815. E-mail: dcrick{at}cvmbs.colostate.edu.

Journal of Bacteriology, October 2000, p. 5771-5778, Vol. 182, No. 20
0021-9193/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.


This article has been cited by other articles:

  • Scherman, H., Kaur, D., Pham, H., Skovierova, H., Jackson, M., Brennan, P. J. (2009). Identification of a Polyprenylphosphomannosyl Synthase Involved in the Synthesis of Mycobacterial Mannosides. J. Bacteriol. 191: 6769-6772 [Abstract] [Full Text]  
  • Belanova, M., Dianiskova, P., Brennan, P. J., Completo, G. C., Rose, N. L., Lowary, T. L., Mikusova, K. (2008). Galactosyl Transferases in Mycobacterial Cell Wall Synthesis. J. Bacteriol. 190: 1141-1145 [Abstract] [Full Text]  
  • Cervantes-Cervantes, M., Gallagher, C. E., Zhu, C., Wurtzel, E. T. (2006). Maize cDNAs Expressed in Endosperm Encode Functional Farnesyl Diphosphate Synthase with Geranylgeranyl Diphosphate Synthase Activity. Plant Physiol. 141: 220-231 [Abstract] [Full Text]  
  • Mahapatra, S., Yagi, T., Belisle, J. T., Espinosa, B. J., Hill, P. J., McNeil, M. R., Brennan, P. J., Crick, D. C. (2005). Mycobacterial Lipid II Is Composed of a Complex Mixture of Modified Muramyl and Peptide Moieties Linked to Decaprenyl Phosphate. J. Bacteriol. 187: 2747-2757 [Abstract] [Full Text]  
  • Dhiman, R. K., Schulbach, M. C., Mahapatra, S., Baulard, A. R., Vissa, V., Brennan, P. J., Crick, D. C. (2004). Identification of a novel class of {omega},E,E-farnesyl diphosphate synthase from Mycobacterium tuberculosis. J. Lipid Res. 45: 1140-1147 [Abstract] [Full Text]  
  • Cowlishaw, D. A., Smith, M. C. M. (2002). A Gene Encoding a Homologue of Dolichol Phosphate-{beta}-D-Mannose Synthase Is Required for Infection of Streptomyces coelicolor A3(2) by Phage {phi}C31. J. Bacteriol. 184: 6081-6083 [Abstract] [Full Text]  
  • Crick, D. C., Mahapatra, S., Brennan, P. J. (2001). Biosynthesis of the arabinogalactan-peptidoglycan complex of Mycobacterium tuberculosis. Glycobiology 11: 107R-118R [Abstract] [Full Text]  
  • Schenk, B., Fernandez, F., Waechter, C. J. (2001). The ins(ide) and outs(ide) of dolichyl phosphate biosynthesis and recycling in the endoplasmic reticulum. Glycobiology 11: 61R-70R [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»