Mohammad, Yusuf Ansari and Batra, Sakshi D. and Ojha, Hina and Dhiman, Kanina and Ashish, . and Tyagi, Jaya S and Mande, Shekhar C (2020) A novel function ofMycobacterium tuberculosischaperonin paralog GroEL1 in copper homeostasis. FEBS Letter. ISSN 0014-5793
Full text not available from this repository. (Request a copy)Abstract
Among the two GroEL paralogs inMycobacterium 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 onM. tuberculosisphysiology. 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 stressin 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 inM. tuberculosismight have led to their evolutionary divergence and consequent functional divergence of chaperonins.
| Item Type: | Article |
|---|---|
| Additional Information: | Copyright of this article belongs to Wiley. |
| Uncontrolled Keywords: | copper; GroEL; His‐rich; isothermal titration; calorimetry; Mycobacterium tuberculosis; small angle X‐ray scattering |
| Subjects: | Q Science > QR Microbiology |
| Depositing User: | Dr. K.P.S.Sengar |
| Date Deposited: | 30 Sep 2020 04:34 |
| Last Modified: | 30 Sep 2020 04:34 |
| URI: | http://crdd.osdd.net/open/id/eprint/2607 |
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