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

Venkateswarlu Popuri; Deborah L Croteau; Vilhelm A Bohr

doi:10.1016/j.dnarep.2010.02.012

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

Venkateswarlu Popuri, Deborah L Croteau, Vilhelm A Bohr

14 Citations (Scopus)

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.

Original language	English
Journal	DNA Repair
Volume	9
Issue number	6
Pages (from-to)	636-42
Number of pages	7
DOIs	https://doi.org/10.1016/j.dnarep.2010.02.012
Publication status	Published - 4 Jun 2010

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

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10.1016/j.dnarep.2010.02.012

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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}",

year = "2010",

month = jun,

day = "4",

doi = "10.1016/j.dnarep.2010.02.012",

language = "English",

volume = "9",

pages = "636--42",

journal = "DNA Repair",

issn = "1568-7856",

publisher = "Elsevier",

number = "6",

}

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

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

SN - 1568-7856

VL - 9

SP - 636

EP - 642

JO - DNA Repair

JF - DNA Repair

IS - 6

ER -

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

Abstract

Keywords

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