Oxanine DNA glycosylase activities in mammalian systems

被引：11

作者：

Dong, Liang ^{[1
]}

Meira, Lisiane B. ^{[2
]}

Hazra, Tapas K. ^{[3
,4
]}

Samson, Leona D. ^{[2
]}

Cao, Weiguo ^{[1
]}

机构：

[1] Clemson Univ, Dept Genet & Biochem, S Carolina Expt Stn, Clemson, SC 29634 USA

[2] MIT, Biol Engn Div, Cambridge, MA 02139 USA

[3] Univ Texas Galveston, Med Branch, Scaly Ctr Mol Sci & Biochem, Galveston, TX 77555 USA

[4] Univ Texas Galveston, Med Branch, Scaly Ctr Mol Bol, Galveston, TX 77555 USA

来源：

DNA REPAIR | 2008年 / 7卷 / 01期

关键词：

deamination; oxanine DNA glycosylase; AAG; NEIL1; SMUG1; mammals;

D O I：

10.1016/j.dnarep.2007.09.004

中图分类号：

Q3 [遗传学];

学科分类号：

071007 ; 090102 ;

摘要：

DNA bases carrying an exocyclic amino group, namely adenine (A), guanine (G) and cytosine (C), encounter deamination under nitrosative stress. Oxanine (O), derived from deamination of guanine, is a cytotoxic and potentially mutagenic lesion and studies of its enzymatic repair are limited. Previously, we reported that the murine alkyladenine glycosylase (Aag) acts as an oxanine DNA glycosylase (JBC (2004), 279: 38177). Here, we report our recent findings on additional oxanine DNA glycosylase (ODG) activities in Aag knockout mouse tissues and other mammalian tissues. Analysis of the partially purified proteins from the mammalian cell extracts indicated the existence of ODG enzymes in addition to Aag. Data obtained from oxanine DNA cleavage assays using purified human glycosylases demonstrated that two known glycosylases, hNEIL1 and hSMUG1, contained weak but detectable ODG activities. ODG activity was the highest in hAAG and lowest in hSMUG1. (C) 2007 Elsevier B.V. All rights reserved.

引用

页码：128 / 134

页数：7

共 35 条

[11] Identification and characterization of a human DNA glycosylase for repair of modified bases in oxidatively damaged DNA [J].

Hazra, TK ;

Izumi, T ;

Boldogh, I ;

Imhoff, B ;

Kow, YW ;

Jaruga, P ;

Dizdaroglu, M ;

Mitra, S .

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2002, 99 (06) :3523-3528

[12] Oxanine DNA glycosylase activity from mammalian alkyladenine glycosylase [J].

Hitchcock, TM ;

Dong, L ;

Connor, EE ;

Meira, LB ;

Samson, LD ;

Wyatt, MD ;

Cao, WG .

JOURNAL OF BIOLOGICAL CHEMISTRY, 2004, 279 (37) :38177-38183

[13] Cleavage of deoxyoxanosine-containing oligodeoxyribonucleotides by bacterial endonuclease V [J].

Hitchcock, TM ;

Gao, HH ;

Cao, WG .

NUCLEIC ACIDS RESEARCH, 2004, 32 (13) :4071-4080

[14] INSTABILITY AND DECAY OF THE PRIMARY STRUCTURE OF DNA [J].

LINDAHL, T .

NATURE, 1993, 362 (6422) :709-715

[15] Efficient nitroso group transfer from N-nitrosoindoles to nucleotides and 2′-deoxyguanosine at physiological pH -: A new pathway for N-nitrosocompounds to exert genotoxicity [J].

Lucas, LT ;

Gatehouse, D ;

Shuker, DEG .

JOURNAL OF BIOLOGICAL CHEMISTRY, 1999, 274 (26) :18319-18326

[16] Mammalian 5-Formyluracil-DNA glycosylase. 2. Role of SMUG1 uracil-DNA glycosylase in repair of 5-formyluracil and other oxidized and deaminated base lesions [J].

Masaoka, A ;

Matsubara, M ;

Hasegawa, R ;

Tanaka, T ;

Kurisu, S ;

Terato, H ;

Ohyama, Y ;

Karino, N ;

Matsuda, A ;

Ide, H .

BIOCHEMISTRY, 2003, 42 (17) :5003-5012

[17] Mutational analysis of the damage-recognition and catalytic mechanism of human SMUG1 DNA glycosylase [J].

Matsubara, M ;

Tanaka, T ;

Terato, H ;

Ohmae, E ;

Izumi, S ;

Katayanagi, K ;

Ide, H .

NUCLEIC ACIDS RESEARCH, 2004, 32 (17) :5291-5302

[18] Mammalian 5-formyluracil-DNA glycosylase. 1. Identification and characterization of a novel activity that releases 5-formyluracil from DNA [J].

Matsubara, M ;

Masaoka, A ;

Tanaka, T ;

Miyano, T ;

Kato, N ;

Terato, H ;

Ohyama, Y ;

Iwai, S ;

Ide, H .

BIOCHEMISTRY, 2003, 42 (17) :4993-5002

[19] Stimulation of DNA glycosylase activity of OGG1 by NEIL1: Functional collaboration between two human DNA glycosylases [J].

Mokkapati, SK ;

Wiederhold, L ;

Hazra, TK ;

Mitra, S .

BIOCHEMISTRY, 2004, 43 (36) :11596-11604

[20] Repair activity of base and nucleotide excision repair enzymes for guanine lesions induced by nitrosative stress [J].

Nakano, T ;

Katafuchi, A ;

Shimizu, R ;

Terato, H ;

Suzuki, T ;

Tauchi, H ;

Makino, K ;

Skorvaga, M ;

Van Houten, B ;

Ide, H .

NUCLEIC ACIDS RESEARCH, 2005, 33 (07) :2181-2191

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