Substrate specific stimulation of NEIL1 by WRN but not the other human RecQ helicases

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Substrate specific stimulation of NEIL1 by WRN but not the other human RecQ helicases. / Popuri, Venkateswarlu; Croteau, Deborah L; Bohr, Vilhelm A.

In: DNA Repair, Vol. 9, No. 6, 04.06.2010, p. 636-42.

Research output: Contribution to journalJournal articleResearchpeer-review

Harvard

Popuri, V, Croteau, DL & Bohr, VA 2010, 'Substrate specific stimulation of NEIL1 by WRN but not the other human RecQ helicases', DNA Repair, vol. 9, no. 6, pp. 636-42. https://doi.org/10.1016/j.dnarep.2010.02.012

APA

Popuri, V., Croteau, D. L., & Bohr, V. A. (2010). Substrate specific stimulation of NEIL1 by WRN but not the other human RecQ helicases. DNA Repair, 9(6), 636-42. https://doi.org/10.1016/j.dnarep.2010.02.012

Vancouver

Popuri V, Croteau DL, Bohr VA. Substrate specific stimulation of NEIL1 by WRN but not the other human RecQ helicases. DNA Repair. 2010 Jun 4;9(6):636-42. https://doi.org/10.1016/j.dnarep.2010.02.012

Author

Popuri, Venkateswarlu ; Croteau, Deborah L ; Bohr, Vilhelm A. / Substrate specific stimulation of NEIL1 by WRN but not the other human RecQ helicases. In: DNA Repair. 2010 ; Vol. 9, No. 6. pp. 636-42.

Bibtex

@article{6a29b1bc53c0450c81bafc54469dc20b,
title = "Substrate specific stimulation of NEIL1 by WRN but not the other human RecQ helicases",
abstract = "NEIL1, the mammalian homolog of Escherichia coli endonuclease VIII, is a DNA glycosylase that repairs ring-fragmented purines, saturated pyrimidines and several oxidative lesions like 5-hydroxyuracil, 5-hydroxycytosine, etc. Previous studies from our laboratory have shown that Werner Syndrome protein (WRN), one of the five human RecQ helicases, stimulates NEIL1 DNA glycosylase activity on oxidative DNA lesions. The goal of this study was to extend this observation and analyze the interaction between NEIL1 and all five human RecQ helicases. The DNA substrate specificity of the interaction between WRN and NEIL1 was also analyzed. The results indicate that WRN is the only human RecQ helicase that stimulates NEIL1 DNA glycosylase activity, and that this stimulation requires a double-stranded DNA substrate.",
keywords = "Base Sequence, DNA, DNA Damage, DNA Glycosylases, DNA-(Apurinic or Apyrimidinic Site) Lyase, Exodeoxyribonucleases, Humans, Oligodeoxyribonucleotides, Oxidative Stress, Protein Binding, Pyrimidines, RecQ Helicases, Substrate Specificity, Uracil",
author = "Venkateswarlu Popuri and Croteau, {Deborah L} and Bohr, {Vilhelm A}",
note = "Copyright 2010. Published by Elsevier B.V.",
year = "2010",
month = "6",
day = "4",
doi = "10.1016/j.dnarep.2010.02.012",
language = "English",
volume = "9",
pages = "636--42",
journal = "D N A Repair",
issn = "1568-7864",
publisher = "Elsevier",
number = "6",

}

RIS

TY - JOUR

T1 - Substrate specific stimulation of NEIL1 by WRN but not the other human RecQ helicases

AU - Popuri, Venkateswarlu

AU - Croteau, Deborah L

AU - Bohr, Vilhelm A

N1 - Copyright 2010. Published by Elsevier B.V.

PY - 2010/6/4

Y1 - 2010/6/4

N2 - NEIL1, the mammalian homolog of Escherichia coli endonuclease VIII, is a DNA glycosylase that repairs ring-fragmented purines, saturated pyrimidines and several oxidative lesions like 5-hydroxyuracil, 5-hydroxycytosine, etc. Previous studies from our laboratory have shown that Werner Syndrome protein (WRN), one of the five human RecQ helicases, stimulates NEIL1 DNA glycosylase activity on oxidative DNA lesions. The goal of this study was to extend this observation and analyze the interaction between NEIL1 and all five human RecQ helicases. The DNA substrate specificity of the interaction between WRN and NEIL1 was also analyzed. The results indicate that WRN is the only human RecQ helicase that stimulates NEIL1 DNA glycosylase activity, and that this stimulation requires a double-stranded DNA substrate.

AB - NEIL1, the mammalian homolog of Escherichia coli endonuclease VIII, is a DNA glycosylase that repairs ring-fragmented purines, saturated pyrimidines and several oxidative lesions like 5-hydroxyuracil, 5-hydroxycytosine, etc. Previous studies from our laboratory have shown that Werner Syndrome protein (WRN), one of the five human RecQ helicases, stimulates NEIL1 DNA glycosylase activity on oxidative DNA lesions. The goal of this study was to extend this observation and analyze the interaction between NEIL1 and all five human RecQ helicases. The DNA substrate specificity of the interaction between WRN and NEIL1 was also analyzed. The results indicate that WRN is the only human RecQ helicase that stimulates NEIL1 DNA glycosylase activity, and that this stimulation requires a double-stranded DNA substrate.

KW - Base Sequence

KW - DNA

KW - DNA Damage

KW - DNA Glycosylases

KW - DNA-(Apurinic or Apyrimidinic Site) Lyase

KW - Exodeoxyribonucleases

KW - Humans

KW - Oligodeoxyribonucleotides

KW - Oxidative Stress

KW - Protein Binding

KW - Pyrimidines

KW - RecQ Helicases

KW - Substrate Specificity

KW - Uracil

U2 - 10.1016/j.dnarep.2010.02.012

DO - 10.1016/j.dnarep.2010.02.012

M3 - Journal article

C2 - 20346739

VL - 9

SP - 636

EP - 642

JO - D N A Repair

JF - D N A Repair

SN - 1568-7864

IS - 6

ER -

ID: 33492016