Edited by R.S. Buxton
Thiol specific oxidative stress response in Mycobacteria
Article first published online: 9 JAN 2006
DOI: 10.1016/j.femsle.2005.06.004
Additional Information
How to Cite
Dosanjh, N. S., Rawat, M., Chung, J.-H. and Av-Gay, Y. (2005), Thiol specific oxidative stress response in Mycobacteria. FEMS Microbiology Letters, 249: 87–94. doi: 10.1016/j.femsle.2005.06.004
Publication History
- Issue published online: 9 JAN 2006
- Article first published online: 9 JAN 2006
- Received 17 March 2005, Revised 31 May 2005, Accepted 2 June 2005
- Abstract
- Article
- References
- Cited By
Keywords:
- Mycothiol;
- Diamide;
- Mycobacteria;
- Disulfide
Abstract
The cellular response of mycobacteria to thiol specific oxidative stress was studied in Mycobacterium bovis BCG cultures. Two-dimensional gel electrophoresis revealed that upon diamide treatment at least 60 proteins were upregulated. Fourteen of these proteins were identified by MALDI-MS; four proteins, AhpC, Tpx, GroEL2, and GroEL1 are functionally related to oxidative stress response; eight proteins, LeuC, LeuD, Rv0224c, Rv3029c, AsnB, Rv2971, PheA and HisH are classified as part of the bacterial intermediary metabolism and respiration pathways; protein EchA14 belong to lipid metabolism, and NrdE, belongs to the mycobacterial information pathway category. Reverse transcription followed by quantitative real time PCR in response to diamide stress demonstrated that protein expression is directly proportional to the corresponding gene transcription.

1574-6968/asset/FML_left.gif?v=1&s=d9ad90a5f75253894fe5059aa2f75bf910ebf83a)
1574-6968/asset/FML_right.gif?v=1&s=48d5e33deef512c09651020f71074ad93d3351e7)
1574-6968/asset/cover.gif?v=1&s=069bb2c224e243333d4486580fbd90d9ebeffa6b)