TY  - JOUR
N1  - Copyright of this article belongs to Wiley.
ID  - open2607
UR  - https://febs.onlinelibrary.wiley.com/doi/abs/10.1002/1873-3468.13906
A1  - Mohammad, Yusuf Ansari
A1  - Batra, Sakshi D.
A1  - Ojha, Hina
A1  - Dhiman, Kanina
A1  - Ashish, .
A1  - Tyagi, Jaya S
A1  - Mande, Shekhar C
Y1  - 2020/09//
N2  - 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.
PB  - WILEY-V C H VERLAG GMBH
JF  - FEBS Letter
KW  - copper; GroEL; His?rich; isothermal titration; calorimetry; Mycobacterium tuberculosis; small angle X?ray scattering
SN  - 0014-5793
TI  - A novel function ofMycobacterium tuberculosischaperonin paralog GroEL1 in copper homeostasis
ER  -