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Journal of Bacteriology, October 2008, p. 6795-6804, Vol. 190, No. 20
0021-9193/08/$08.00+0     doi:10.1128/JB.00401-08
Copyright © 2008, American Society for Microbiology. All Rights Reserved.

O2- and NO-Sensing Mechanism through the DevSR Two-Component System in Mycobacterium smegmatis{triangledown}

Jin-Mok Lee,1 Ha Yeon Cho,2 Hyo Je Cho,2 In-Jeong Ko,3 Sae Woong Park,4 Hyung-Suk Baik,1 Jee-Hyun Oh,5 Chi-Yong Eom,5 Young Min Kim,4 Beom Sik Kang,2* and Jeong-Il Oh1*

Department of Microbiology, Pusan National University, 609-735 Busan, South Korea,1 School of Life Science and Biotechnology, Kyungpook National University, 702-701 Daegu, South Korea,2 Korea Science Academy, 614-822 Busan, South Korea,3 Department of Biology, Yonsei University, 120-749 Seoul, South Korea,4 Korea Basic Science Institute, Daejeon, South Korea5

Received 21 March 2008/ Accepted 5 August 2008

The DevS histidine kinase of Mycobacterium smegmatis contains tandem GAF domains (GAF-A and GAF-B) in its N-terminal sensory domain. The heme iron of DevS is in the ferrous state when purified and is resistant to autooxidation from a ferrous to a ferric state in the presence of O2. The redox property of the heme and the results of sequence comparison analysis indicate that DevS of M. smegmatis is more closely related to DosT of Mycobacterium tuberculosis than DevS of M. tuberculosis. The binding of O2 to the deoxyferrous heme led to a decrease in the autokinase activity of DevS, whereas NO binding did not. The regulation of DevS autokinase activity in response to O2 and NO was not observed in the DevS derivatives lacking its heme, indicating that the ligand-binding state of the heme plays an important role in the regulation of DevS kinase activity. The redox state of the quinone/quinol pool of the respiratory electron transport chain appears not to be implicated in the regulation of DevS activity. Neither cyclic GMP (cGMP) nor cAMP affected DevS autokinase activity, excluding the possibility that the cyclic nucleotides serve as the effector molecules to modulate DevS kinase activity. The three-dimensional structure of the putative GAF-B domain revealed that it has a GAF folding structure without cyclic nucleotide binding capacity.

* Corresponding author. Mailing address for J. I. Oh: Department of Microbiology, Pusan National University, 609-735 Busan, South Korea. Phone: 82-51-510-2593. Fax: 82-51-514-1778. E-mail: joh{at}pusan.ac.kr. Mailing address for B. S. Kang: School of Life Science and Biotechnology, Kyungpook National University, 702-701 Daegu, South Korea. Phone: 82-53-950-6357. Fax: 82-53-943-2762. E-mail: bskang2{at}knu.ac.kr

{triangledown} Published ahead of print on 15 August 2008.

Journal of Bacteriology, October 2008, p. 6795-6804, Vol. 190, No. 20
0021-9193/08/$08.00+0     doi:10.1128/JB.00401-08
Copyright © 2008, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Cho, H. Y., Cho, H. J., Kim, Y. M., Oh, J. I., Kang, B. S. (2009). Structural Insight into the Heme-based Redox Sensing by DosS from Mycobacterium tuberculosis. J. Biol. Chem. 284: 13057-13067 [Abstract] [Full Text]  


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