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A novel function ofMycobacterium tuberculosischaperonin paralog GroEL1 in copper homeostasis

DIR@IMTECH: CSIR-Institute of Microbial Technology

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Title A novel function ofMycobacterium tuberculosischaperonin paralog GroEL1 in copper homeostasis
 
Creator Mohammad, Yusuf Ansari
Batra, Sakshi D.
Ojha, Hina
Dhiman, Kanina
Ashish, .
Tyagi, Jaya S
Mande, Shekhar C
 
Subject QR Microbiology
 
Description 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.
 
Publisher WILEY-V C H VERLAG GMBH
 
Date 2020-09
 
Type Article
PeerReviewed
 
Relation https://febs.onlinelibrary.wiley.com/doi/abs/10.1002/1873-3468.13906
http://crdd.osdd.net/open/2607/
 
Identifier 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