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Regulation of the human Suv3 helicase on DNA by inorganic cofactors

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Regulation of the human Suv3 helicase on DNA by inorganic cofactors. / Venø, Susanne T; Witt, Marie B; Kulikowicz, Tomasz; Bohr, Vilhelm A; Stevnsner, Tinna.

In: Biochimie, Vol. 108, 01.2015, p. 160-168.

Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaperJournal articleResearchpeer-review

Harvard

Venø, ST, Witt, MB, Kulikowicz, T, Bohr, VA & Stevnsner, T 2015, 'Regulation of the human Suv3 helicase on DNA by inorganic cofactors', Biochimie, vol. 108, pp. 160-168. https://doi.org/10.1016/j.biochi.2014.11.003

APA

Venø, S. T., Witt, M. B., Kulikowicz, T., Bohr, V. A., & Stevnsner, T. (2015). Regulation of the human Suv3 helicase on DNA by inorganic cofactors. Biochimie, 108, 160-168. https://doi.org/10.1016/j.biochi.2014.11.003

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MLA

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Author

Venø, Susanne T ; Witt, Marie B ; Kulikowicz, Tomasz ; Bohr, Vilhelm A ; Stevnsner, Tinna. / Regulation of the human Suv3 helicase on DNA by inorganic cofactors. In: Biochimie. 2015 ; Vol. 108. pp. 160-168.

Bibtex

@article{93fddb15426e4284b8d878631d1c5c45,
title = "Regulation of the human Suv3 helicase on DNA by inorganic cofactors",
abstract = "Mitochondria are essential organelles and consequently proper expression and maintenance of the mitochondrial genome are indispensable for proper cell function. The mitochondrial Suv3 (SUPV3L1) helicase is known to have a central role in mitochondrial RNA metabolism and to be essential for maintenance of mitochondrial DNA stability. Here we have performed biochemical investigations to determine the potential regulation of the human Suv3 (hSuv3) helicase function by inorganic cofactors. We find that hSuv3 helicase and ATPase activity in vitro is strictly dependent on the presence of specific divalent cations. Interestingly, we show that divalent cations and nucleotide concentration have a direct effect on helicase substrate stability. Also, hSuv3 helicase is able to utilize several different nucleotide cofactors including both NTPs and dNTPs. Intriguingly, the potency of the individual nucleotide as energy source for hSuv3 unwinding differed depending on the included divalent cation and nucleotide concentration. At low concentrations, all four NTPs could support helicase activity with varying effectiveness depending on the included divalent cation. However, at higher nucleotide concentrations, only ATP was able to elicit the helicase activity of hSuv3. Consequently, we speculate that the capacity of hSuv3 DNA unwinding activity might be sensitive to the local availability of specific inorganic cofactors.",
author = "Ven{\o}, {Susanne T} and Witt, {Marie B} and Tomasz Kulikowicz and Bohr, {Vilhelm A} and Tinna Stevnsner",
note = "Copyright {\textcopyright} 2014 Elsevier B.V. and Soci{\'e}t{\'e} fran{\c c}aise de biochimie et biologie Mol{\'e}culaire (SFBBM). All rights reserved.",
year = "2015",
month = jan,
doi = "10.1016/j.biochi.2014.11.003",
language = "English",
volume = "108",
pages = "160--168",
journal = "Biochimie",
issn = "0300-9084",
publisher = "Elsevier Masson",

}

RIS

TY - JOUR

T1 - Regulation of the human Suv3 helicase on DNA by inorganic cofactors

AU - Venø, Susanne T

AU - Witt, Marie B

AU - Kulikowicz, Tomasz

AU - Bohr, Vilhelm A

AU - Stevnsner, Tinna

N1 - Copyright © 2014 Elsevier B.V. and Société française de biochimie et biologie Moléculaire (SFBBM). All rights reserved.

PY - 2015/1

Y1 - 2015/1

N2 - Mitochondria are essential organelles and consequently proper expression and maintenance of the mitochondrial genome are indispensable for proper cell function. The mitochondrial Suv3 (SUPV3L1) helicase is known to have a central role in mitochondrial RNA metabolism and to be essential for maintenance of mitochondrial DNA stability. Here we have performed biochemical investigations to determine the potential regulation of the human Suv3 (hSuv3) helicase function by inorganic cofactors. We find that hSuv3 helicase and ATPase activity in vitro is strictly dependent on the presence of specific divalent cations. Interestingly, we show that divalent cations and nucleotide concentration have a direct effect on helicase substrate stability. Also, hSuv3 helicase is able to utilize several different nucleotide cofactors including both NTPs and dNTPs. Intriguingly, the potency of the individual nucleotide as energy source for hSuv3 unwinding differed depending on the included divalent cation and nucleotide concentration. At low concentrations, all four NTPs could support helicase activity with varying effectiveness depending on the included divalent cation. However, at higher nucleotide concentrations, only ATP was able to elicit the helicase activity of hSuv3. Consequently, we speculate that the capacity of hSuv3 DNA unwinding activity might be sensitive to the local availability of specific inorganic cofactors.

AB - Mitochondria are essential organelles and consequently proper expression and maintenance of the mitochondrial genome are indispensable for proper cell function. The mitochondrial Suv3 (SUPV3L1) helicase is known to have a central role in mitochondrial RNA metabolism and to be essential for maintenance of mitochondrial DNA stability. Here we have performed biochemical investigations to determine the potential regulation of the human Suv3 (hSuv3) helicase function by inorganic cofactors. We find that hSuv3 helicase and ATPase activity in vitro is strictly dependent on the presence of specific divalent cations. Interestingly, we show that divalent cations and nucleotide concentration have a direct effect on helicase substrate stability. Also, hSuv3 helicase is able to utilize several different nucleotide cofactors including both NTPs and dNTPs. Intriguingly, the potency of the individual nucleotide as energy source for hSuv3 unwinding differed depending on the included divalent cation and nucleotide concentration. At low concentrations, all four NTPs could support helicase activity with varying effectiveness depending on the included divalent cation. However, at higher nucleotide concentrations, only ATP was able to elicit the helicase activity of hSuv3. Consequently, we speculate that the capacity of hSuv3 DNA unwinding activity might be sensitive to the local availability of specific inorganic cofactors.

U2 - 10.1016/j.biochi.2014.11.003

DO - 10.1016/j.biochi.2014.11.003

M3 - Journal article

C2 - 25446650

VL - 108

SP - 160

EP - 168

JO - Biochimie

JF - Biochimie

SN - 0300-9084

ER -