A novel function of Mycobacterium tuberculosis chaperonin paralog GroEL1 in copper homeostasis

Mohammed Yousuf Ansari; Sakshi D. Batra; Hina Ojha; Kanika Dhiman; Ashish Ganguly; Jaya S. Tyagi; Shekhar C. Mande

doi:10.1002/1873-3468.13906

A novel function of Mycobacterium tuberculosis chaperonin paralog GroEL1 in copper homeostasis

Mohammed Yousuf Ansari
, Sakshi D. Batra
, Hina Ojha
, Kanika Dhiman
, Ashish Ganguly
, Jaya S. Tyagi
, Shekhar C. Mande

Research output: Contribution to journal › Article › peer-review

14 Scopus citations

Abstract

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.

Original language	English
Pages (from-to)	3305-3323
Number of pages	19
Journal	FEBS Letters
Volume	594
Issue number	20
DOIs	https://doi.org/10.1002/1873-3468.13906
State	Published - 1 Oct 2020
Externally published	Yes

Keywords

GroEL
His-rich
Mycobacterium tuberculosis
copper
isothermal titration calorimetry
small angle X-ray scattering

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10.1002/1873-3468.13906

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title = "A novel function of Mycobacterium tuberculosis chaperonin paralog GroEL1 in copper homeostasis",

abstract = "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.",

keywords = "GroEL, His-rich, Mycobacterium tuberculosis, copper, isothermal titration calorimetry, small angle X-ray scattering",

author = "Ansari, \{Mohammed Yousuf\} and Batra, \{Sakshi D.\} and Hina Ojha and Kanika Dhiman and Ashish Ganguly and Tyagi, \{Jaya S.\} and Mande, \{Shekhar C.\}",

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doi = "10.1002/1873-3468.13906",

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T1 - A novel function of Mycobacterium tuberculosis chaperonin paralog GroEL1 in copper homeostasis

AU - Ansari, Mohammed Yousuf

AU - Batra, Sakshi D.

AU - Ojha, Hina

AU - Dhiman, Kanika

AU - Ganguly, Ashish

AU - Tyagi, Jaya S.

AU - Mande, Shekhar C.

PY - 2020/10/1

Y1 - 2020/10/1

N2 - 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.

AB - 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.

KW - GroEL

KW - His-rich

KW - Mycobacterium tuberculosis

KW - copper

KW - isothermal titration calorimetry

KW - small angle X-ray scattering

UR - https://www.scopus.com/pages/publications/85090946345

U2 - 10.1002/1873-3468.13906

DO - 10.1002/1873-3468.13906

M3 - Article

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AN - SCOPUS:85090946345

SN - 0014-5793

VL - 594

SP - 3305

EP - 3323

JO - FEBS Letters

JF - FEBS Letters

IS - 20

ER -

A novel function of Mycobacterium tuberculosis chaperonin paralog GroEL1 in copper homeostasis

Abstract

Keywords

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