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Characterization of Recombinant Endonuclease IV from Mycobacterium tuberculosis

Authors
  • Dymova, M. A.1
  • Endutkin, A. V.1
  • Polunovsky, V. V.2
  • Zakabunin, A. I.1
  • Khrapov, E. A.1
  • Torgasheva, N. A.1
  • Yudkina, A. V.1
  • Mechetin, G. V.1
  • Filipenko, M. L.1
  • Zharkov, D. O.1, 2
  • 1 Institute of Chemical Biology and Fundamental Medicine, Siberian Branch, Russian Academy of Sciences, Novosibirsk, 630090, Russia , Novosibirsk (Russia)
  • 2 Novosibirsk State University, Novosibirsk, 630090, Russia , Novosibirsk (Russia)
Type
Published Article
Journal
Molecular Biology
Publisher
Pleiades Publishing
Publication Date
Mar 01, 2021
Volume
55
Issue
2
Pages
225–233
Identifiers
DOI: 10.1134/S0026893321020059
Source
Springer Nature
Keywords
License
Yellow

Abstract

AbstractMycobacterium tuberculosis cells contain two apurinic/apyrimidinic (AP) endonucleases, endonuclease IV (MtbEnd) and exonuclease III (MtbXthA), the former playing a dominant role in protecting mycobacterial DNA from oxidative stress. Mycobacterial endonuclease IV substantially differs from its homologs found in Escherichia coli and other proteobacteria in a number of conserved positions important for DNA binding and AP site recognition. The M. tuberculosis end gene was cloned, and recombinant MtbEnd purified and characterized. The protein efficiently hydrolyzed DNA at the natural AP site and its 1′-deoxy analog in the presence of divalent cations, of which Ca2+, Mn2+, and Co2+ supported the highest activity. Exonuclease activity was not detected in MtbEnt preparations. The pH optimum was estimated at 7.0–8.0; the ionic strength optimum, at ~50 mM NaCl. Enzymatic activity of MtbEnd was suppressed in the presence of methoxyamine, a chemotherapeutic agent that modifies AP sites. Based on the results, MtbEnd was assumed to provide a possible target for new anti-tuberculosis drugs.

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