A novel function of Mycobacterium tuberculosis chaperonin paralog GroEL1 in copper homeostasis
| Autor: | Mohammed Yousuf Ansari, Jaya Sivaswami Tyagi, Sakshi Dhingra Batra, Kanika Dhiman, Hina Ojha, Shekhar C. Mande, Ashish Ganguly |
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| Rok vydání: | 2020 |
| Předmět: |
Models
Molecular Protein Conformation Biophysics Biochemistry Models Biological Anilino Naphthalenesulfonates Chaperonin Mycobacterium tuberculosis 03 medical and health sciences Gene Knockout Techniques X-Ray Diffraction Structural Biology Scattering Small Angle Genetics Homeostasis Histidine Viability assay Amino Acid Sequence Gene Silencing Molecular Biology Gene 030304 developmental biology 0303 health sciences Binding Sites biology Sequence Homology Amino Acid Chemistry 030302 biochemistry & molecular biology Isothermal titration calorimetry Cell Biology Chaperonin 60 biology.organism_classification GroEL Structural Homology Protein Thermodynamics Oxidation-Reduction Functional divergence Copper DNA Damage |
| Zdroj: | FEBS lettersReferences. 594(20) |
| ISSN: | 1873-3468 |
| Popis: | Among the two GroEL paralogs in Mycobacterium tuberculosis, GroEL1 and GroEL2, GroEL1 has a characteristic histidine-rich C terminus. Since histidine richness is likely to be involved in metal binding, we attempted to decipher the role of GroEL1 in chelating metals and the consequence on M. tuberculosis physiology. Isothermal titration calorimetry showed that GroEL1 binds copper and other metals. Mycobacterial viability assay, redox balance, and DNA protection assay concluded that GroEL1 protects from copper stress in vitro. Solution X-ray scattering and constrained modeling of GroEL1 -/+ copper ions showed reorientation of the apical domain as seen in functional assembly. We conclude that the duplication of chaperonin genes in M. tuberculosis might have led to their evolutionary divergence and consequent functional divergence of chaperonins. |
| Databáze: | OpenAIRE |
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