Результаты исследований: Научные публикации в периодических изданиях › статья › Рецензирование
Characterization of Recombinant Endonuclease IV from Mycobacterium tuberculosis. / Dymova, M. A.; Endutkin, A. V.; Polunovsky, V. V. и др.
в: Molecular Biology, Том 55, № 2, 03.2021, стр. 225-233.Результаты исследований: Научные публикации в периодических изданиях › статья › Рецензирование
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TY - JOUR
T1 - Characterization of Recombinant Endonuclease IV from Mycobacterium tuberculosis
AU - Dymova, M. A.
AU - Endutkin, A. V.
AU - Polunovsky, V. V.
AU - Zakabunin, A. I.
AU - Khrapov, E. A.
AU - Torgasheva, N. A.
AU - Yudkina, A. V.
AU - Mechetin, G. V.
AU - Filipenko, M. L.
AU - Zharkov, D. O.
N1 - Funding Information: This work was supported by the Program of Basic Research at State Academies of Sciences (project nos. AAAA-A17-117020210027-9 (MtbEnd cloning and purification), AAAA-A17-117020210023-1 (MtbEnd characterization), and FSUS-2020-0035 (bioinformatics analyses and molecular modeling of the Nfo proteins)). Sequencing was performed at the Genomics Core Facility (Siberian Branch, Russian Academy of Sciences). Publisher Copyright: © 2021, Pleiades Publishing, Inc. Copyright: Copyright 2021 Elsevier B.V., All rights reserved.
PY - 2021/3
Y1 - 2021/3
N2 - Mycobacterium 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.
AB - Mycobacterium 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.
KW - AP endonuclease
KW - DNA repair
KW - methoxyamine
KW - Mycobacterium tuberculosis
UR - http://www.scopus.com/inward/record.url?scp=85105015479&partnerID=8YFLogxK
U2 - 10.1134/S0026893321020059
DO - 10.1134/S0026893321020059
M3 - Article
AN - SCOPUS:85105015479
VL - 55
SP - 225
EP - 233
JO - Molecular Biology
JF - Molecular Biology
SN - 0026-8933
IS - 2
ER -
ID: 28453742