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A novel function of Mycobacterium tuberculosis chaperonin paralog GroEL1 in copper homeostasis
Author(s) -
Ansari Mohammed Yousuf,
Batra Sakshi D.,
Ojha Hina,
Dhiman Kanika,
Ganguly Ashish,
Tyagi Jaya S.,
Mande Shekhar C.
Publication year - 2020
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1002/1873-3468.13906
Subject(s) - isothermal titration calorimetry , chaperonin , mycobacterium tuberculosis , groel , histidine , groes , biochemistry , copper , heat shock protein , biology , chemistry , protein folding , biophysics , tuberculosis , gene , escherichia coli , enzyme , medicine , organic chemistry , pathology
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.