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Characterization of Recombinant Endonuclease IV from Mycobacterium tuberculosis. / Dymova, M. A.; Endutkin, A. V.; Polunovsky, V. V. et al.

In: Molecular Biology, Vol. 55, No. 2, 03.2021, p. 225-233.

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

Harvard

Dymova, MA, Endutkin, AV, Polunovsky, VV, Zakabunin, AI, Khrapov, EA, Torgasheva, NA, Yudkina, AV, Mechetin, GV, Filipenko, ML & Zharkov, DO 2021, 'Characterization of Recombinant Endonuclease IV from Mycobacterium tuberculosis', Molecular Biology, vol. 55, no. 2, pp. 225-233. https://doi.org/10.1134/S0026893321020059

APA

Dymova, M. A., Endutkin, A. V., Polunovsky, V. V., Zakabunin, A. I., Khrapov, E. A., Torgasheva, N. A., Yudkina, A. V., Mechetin, G. V., Filipenko, M. L., & Zharkov, D. O. (2021). Characterization of Recombinant Endonuclease IV from Mycobacterium tuberculosis. Molecular Biology, 55(2), 225-233. https://doi.org/10.1134/S0026893321020059

Vancouver

Dymova MA, Endutkin AV, Polunovsky VV, Zakabunin AI, Khrapov EA, Torgasheva NA et al. Characterization of Recombinant Endonuclease IV from Mycobacterium tuberculosis. Molecular Biology. 2021 Mar;55(2):225-233. doi: 10.1134/S0026893321020059

Author

Dymova, M. A. ; Endutkin, A. V. ; Polunovsky, V. V. et al. / Characterization of Recombinant Endonuclease IV from Mycobacterium tuberculosis. In: Molecular Biology. 2021 ; Vol. 55, No. 2. pp. 225-233.

BibTeX

@article{15e33590b69847ac96b8bd5b427e90f6,
title = "Characterization of Recombinant Endonuclease IV from Mycobacterium tuberculosis",
abstract = "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.",
keywords = "AP endonuclease, DNA repair, methoxyamine, Mycobacterium tuberculosis",
author = "Dymova, {M. A.} and Endutkin, {A. V.} and Polunovsky, {V. V.} and Zakabunin, {A. I.} and Khrapov, {E. A.} and Torgasheva, {N. A.} and Yudkina, {A. V.} and Mechetin, {G. V.} and Filipenko, {M. L.} and Zharkov, {D. O.}",
note = "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: {\textcopyright} 2021, Pleiades Publishing, Inc. Copyright: Copyright 2021 Elsevier B.V., All rights reserved.",
year = "2021",
month = mar,
doi = "10.1134/S0026893321020059",
language = "English",
volume = "55",
pages = "225--233",
journal = "Molecular Biology",
issn = "0026-8933",
publisher = "Maik Nauka-Interperiodica Publishing",
number = "2",

}

RIS

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