TAILIEUCHUNG - Báo cáo khoa học: Studies on structural and functional divergence among seven WhiB proteins of Mycobacterium tuberculosis H37Rv

ThewhiB-like genes (1-7) of Mycobacterium tuberculosisare involved in cell division, nutrient starvation, pathogenesis, antibiotic resistance and stress sensing. Although the biochemical properties of WhiB1, WhiB3 and WhiB4 are known, there is no information about the other proteins. | ễFEBS Journal Studies on structural and functional divergence among seven WhiB proteins of Mycobacterium tuberculosis H37Rv Md. Suhail Alam Saurabh K. Garg and Pushpa Agrawal Institute of MicrobialTechnology CSIR Chandigarh India Keywords iron-sulfur cluster Mycobacterium tuberculosis protein disulfide reductase redox system WhiB Correspondence P. Agrawal Institute of Microbial Technology Sector-39A Chandigarh 160 036 India Fax 91 172 269 0585 Tel 91 172 263 6680 263 6681 Ext 3264 E-mail pushpa@ Present address Department of Environmentaland Biomolec- ular Systems Oregon Health and Science University Beaverton OR USA Received 16 September 2008 revised 22 October 2008 accepted 23 October 2008 doi The whB-like genes 1-7 of Mycobacterium tuberculosis are involved in cell division nutrient starvation pathogenesis antibiotic resistance and stress sensing. Although the biochemical properties of WhiBl WhiB3 and WhiB4 are known there is no information about the other proteins. Here we elucidate in detail the biochemical and biophysical properties of WhiB2 WhiB5 WhiB6 and WhiB7 of M. tuberculosis and present a comprehensive comparative study on the molecular properties of all WhiB proteins. UV-Vis spectroscopy has suggested the presence of a redox-sensitive 2Fe-2S cluster in each of the WhiB proteins which remains stably bound to the proteins in the presence of 8 M urea. The 2Fe-2S cluster of each protein was oxidation labile but the rate of cluster loss decreased under reducing environments. The 2Fe-2S cluster of each WhiB protein responded differently to the oxidative effect of air and oxidized glutathione. In all cases disassembly of the 2Fe-2S cluster was coupled with the oxidation of cysteine-thiols and the formation of two intramolecular disulfide bonds. Both CD and fluorescence spectroscopy revealed that WhiB proteins are structurally divergent members of the same family. Similar to WhiB1 WhiB3 and WhiB4 apo WhiB5 WhiB6 .

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