This Article Full Text Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Reprints and Permissions Copyright Information Books from ASM Press MicrobeWorld Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Deol, P. Articles by Singh, Y. Search for Related Content PubMed PubMed Citation Articles by Deol, P. Articles by Singh, Y.

 Previous Article  |  Next Article 

Journal of Bacteriology, May 2005, p. 3415-3420, Vol. 187, No. 10
0021-9193/05/$08.00+0     doi:10.1128/JB.187.10.3415-3420.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.

Role of Mycobacterium tuberculosis Ser/Thr Kinase PknF: Implications in Glucose Transport and Cell Division

Parampal Deol,^1, Reena Vohra,^1, Adesh Kumar Saini,¹ Amit Singh,² Harish Chandra,¹ Puneet Chopra,¹ Taposh K. Das,³ Anil K. Tyagi,² and Yogendra Singh^1*

Institute of Genomics and Integrative Biology, Mall Road, Delhi,¹ Department of Biochemistry, University of Delhi, South Campus, New Delhi,² Department of Anatomy, All India Institute of Medical Sciences, New Delhi, India³

Received 16 December 2004/ Accepted 8 February 2005

Protein kinases have a diverse array of functions in bacterial physiology, with a distinct role in the regulation of development, stress responses, and pathogenicity. pknF, one of the 11 kinases of Mycobacterium tuberculosis, encodes an autophosphorylating, transmembrane serine/threonine protein kinase, which is absent in the fast-growing, nonpathogenic Mycobacterium smegmatis. Herein, we investigate the physiological role of PknF using an antisense strategy with M. tuberculosis and expressing PknF and its kinase mutant (K41M) in M. smegmatis. Expression of PknF in M. smegmatis led to reduction in the growth rate and shortening and swelling of cells with constrictions. Interestingly, an antisense strain of M. tuberculosis expressing a low level of PknF displayed fast growth and a deformed cell morphology compared to the wild-type strain. Electron microscopy showed that most of the cells of the antisense strain were of a smaller size with an aberrant septum. Furthermore, nutrient transport analysis of these strains was conducted using ³H-labeled and ¹⁴C-labeled substrates. A significant increase in the uptake of D-glucose but not of glycerol, leucine, or oleic acid was observed in the antisense strain compared to the wild-type strain. The results suggest that PknF plays a direct/indirect role in the regulation of glucose transport, cell growth, and septum formation in M. tuberculosis.

These authors contributed equally to this work.

This article has been cited by other articles:

• Hett, E. C., Rubin, E. J. (2008). Bacterial Growth and Cell Division: a Mycobacterial Perspective. Microbiol. Mol. Biol. Rev. 72: 126-156 [Abstract] [Full Text]  
• Narayan, A., Sachdeva, P., Sharma, K., Saini, A. K., Tyagi, A. K., Singh, Y. (2007). Serine threonine protein kinases of mycobacterial genus: phylogeny to function. Physiol. Genomics 29: 66-75 [Abstract] [Full Text]  
• Rao, A., Ram, G., Saini, A. K., Vohra, R., Kumar, K., Singh, Y., Ranganathan, A. (2007). Synthesis and Selection of De Novo Proteins That Bind and Impede Cellular Functions of an Essential Mycobacterial Protein. Appl. Environ. Microbiol. 73: 1320-1331 [Abstract] [Full Text]  
• Fernandez, P., Saint-Joanis, B., Barilone, N., Jackson, M., Gicquel, B., Cole, S. T., Alzari, P. M. (2006). The Ser/Thr Protein Kinase PknB Is Essential for Sustaining Mycobacterial Growth. J. Bacteriol. 188: 7778-7784 [Abstract] [Full Text]  
• Raghunand, T. R., Bishai, W. R. (2006). Mycobacterium smegmatis whmD and its homologue Mycobacterium tuberculosis whiB2 are functionally equivalent.. Microbiology 152: 2735-2747 [Abstract] [Full Text]  
• Alderwick, L. J., Molle, V., Kremer, L., Cozzone, A. J., Dafforn, T. R., Besra, G. S., Futterer, K. (2006). Molecular structure of EmbR, a response element of Ser/Thr kinase signaling in Mycobacterium tuberculosis. Proc. Natl. Acad. Sci. USA 103: 2558-2563 [Abstract] [Full Text]