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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Ab Rahman, Nurlilah Binte Berry, Edward A. Jang, Jichan Pethe, Kevin Kim, Mi-sun Huang, Li-shar |
| Description | Author Affiliation: Kim MS ( From the State University of New York Upstate Medical University, Syracuse, New York 13210.); Jang J ( the Institut Pasteur Korea, Sampyeong-dong, Seongnam-si, Gyeonggi-do 463-400, Korea, and.); Ab Rahman NB ( the Lee Kong Chian School of Medicine and School of Biological Sciences, Nanyang Technological University, Singapore 639798, Singapore.); Pethe K ( the Institut Pasteur Korea, Sampyeong-dong, Seongnam-si, Gyeonggi-do 463-400, Korea, and the Lee Kong Chian School of Medicine and School of Biological Sciences, Nanyang Technological University, Singapore 639798, Singapore.); Berry EA ( From the State University of New York Upstate Medical University, Syracuse, New York 13210, berrye@upstate.edu.); Huang LS ( From the State University of New York Upstate Medical University, Syracuse, New York 13210, berryl@upstate.edu.) |
| Abstract | Recently, energy production pathways have been shown to be viable antitubercular drug targets to combat multidrug-resistant tuberculosis and eliminate pathogen in the dormant state. One family of drugs currently under development, the imidazo[1,2-a]pyridine derivatives, is believed to target the pathogen's homolog of the mitochondrial $bc_{1}$ complex. This complex, denoted cytochrome bcc, is highly divergent from mitochondrial Complex III both in subunit structure and inhibitor sensitivity, making it a good target for drug development. There is no soluble cytochrome c in mycobacteria to transport electrons from the bcc complex to cytochrome oxidase. Instead, the bcc complex exists in a “supercomplex” with a cytochrome $aa_{3}-type$ cytochrome oxidase, presumably allowing direct electron transfer. We describe here purification and initial characterization of the mycobacterial cytochrome $bcc-aa_{3}$ supercomplex using a strain of M. smegmatis that has been engineered to express the M. tuberculosis cytochrome bcc. The resulting hybrid supercomplex is stable during extraction and purification in the presence of dodecyl maltoside detergent. It is hoped that this purification procedure will potentiate functional studies of the complex as well as crystallographic studies of drug binding and provide structural insight into a third class of the bc complex superfamily. |
| ISSN | 00219258 |
| e-ISSN | 1083351X |
| Journal | Journal of Biological Chemistry |
| Issue Number | 23 |
| Volume Number | 290 |
| Language | English |
| Publisher | American Society for Biochemistry and Molecular Biology (United States) |
| Publisher Date | 2015-06-05 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | Bacterial Proteins Chemistry Electron Transport Complex III Electron Transport Complex IV Mycobacterium Infections Microbiology Mycobacterium Smegmatis Mycobacterium Tuberculosis Isolation & Purification Electron Transport Research Support, Non-U.S. Gov't Biochemistry Molecular Biology |
| Content Type | Text |
| Resource Type | Article |
| Subject | Cell Biology Biochemistry Molecular Biology |
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