Literature DB >> 11106395

Molecular basis for discriminating between normal and damaged bases by the human alkyladenine glycosylase, AAG.

A Y Lau1, M D Wyatt, B J Glassner, L D Samson, T Ellenberger.   

Abstract

The human 3-methyladenine DNA glycosylase [alkyladenine DNA glycosylase (AAG)] catalyzes the first step of base excision repair by cleaving damaged bases from DNA. Unlike other DNA glycosylases that are specific for a particular type of damaged base, AAG excises a chemically diverse selection of substrate bases damaged by alkylation or deamination. The 2.1-A crystal structure of AAG complexed to DNA containing 1,N(6)-ethenoadenine suggests how modified bases can be distinguished from normal DNA bases in the enzyme active site. Mutational analyses of residues contacting the alkylated base in the crystal structures suggest that the shape of the damaged base, its hydrogen-bonding characteristics, and its aromaticity all contribute to the selective recognition of damage by AAG.

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Year:  2000        PMID： 11106395      PMCID： PMC17617          DOI： 10.1073/pnas.97.25.13573

Source DB:  PubMed          Journal:  Proc Natl Acad Sci U S A        ISSN： 0027-8424            Impact factor:   11.205


  33 in total

1.  Human cDNA expressing a functional DNA glycosylase excising 3-methyladenine and 7-methylguanine.

Authors:  T R O'Connor; J Laval
Journal:  Biochem Biophys Res Commun       Date:  1991-05-15       Impact factor: 3.575

2.  Free R value: a novel statistical quantity for assessing the accuracy of crystal structures.

Authors:  A T Brünger
Journal:  Nature       Date:  1992-01-30       Impact factor: 49.962

3.  Substrate specificity of human methylpurine DNA N-glycosylase.

Authors:  A Asaeda; H Ide; K Asagoshi; S Matsuyama; K Tano; A Murakami; Y Takamori; K Kubo
Journal:  Biochemistry       Date:  2000-02-29       Impact factor: 3.162

Review 4.  Instability and decay of the primary structure of DNA.

Authors:  T Lindahl
Journal:  Nature       Date:  1993-04-22       Impact factor: 49.962

5.  1,N6-ethenoadenine is preferred over 3-methyladenine as substrate by a cloned human N-methylpurine-DNA glycosylase (3-methyladenine-DNA glycosylase).

Authors:  M K Dosanjh; R Roy; S Mitra; B Singer
Journal:  Biochemistry       Date:  1994-02-22       Impact factor: 3.162

6.  Influence of DNA structure on hypoxanthine and 1,N(6)-ethenoadenine removal by murine 3-methyladenine DNA glycosylase.

Authors:  M D Wyatt; L D Samson
Journal:  Carcinogenesis       Date:  2000-05       Impact factor: 4.944

7.  Release of N2,3-ethenoguanine from chloroacetaldehyde-treated DNA by Escherichia coli 3-methyladenine DNA glycosylase II.

Authors:  Z Matijasevic; M Sekiguchi; D B Ludlum
Journal:  Proc Natl Acad Sci U S A       Date:  1992-10-01       Impact factor: 11.205

8.  Conformation of an enzyme-bound substrate of staphylococcal nuclease as determined by NMR.

Authors:  D J Weber; G P Mullen; A S Mildvan
Journal:  Biochemistry       Date:  1991-07-30       Impact factor: 3.162

9.  Saccharomyces cerevisiae 3-methyladenine DNA glycosylase has homology to the AlkA glycosylase of E. coli and is induced in response to DNA alkylation damage.

Authors:  J Chen; B Derfler; L Samson
Journal:  EMBO J       Date:  1990-12       Impact factor: 11.598

10.  Nonenzymatic methylation of DNA by the intracellular methyl group donor S-adenosyl-L-methionine is a potentially mutagenic reaction.

Authors:  B Rydberg; T Lindahl
Journal:  EMBO J       Date:  1982       Impact factor: 11.598
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  93 in total

1.  Distribution patterns of postmortem damage in human mitochondrial DNA.

Authors:  M Thomas P Gilbert; Eske Willerslev; Anders J Hansen; Ian Barnes; Lars Rudbeck; Niels Lynnerup; Alan Cooper
Journal:  Am J Hum Genet       Date:  2002-12-12       Impact factor: 11.025

2.  Direct repair of 3,N(4)-ethenocytosine by the human ALKBH2 dioxygenase is blocked by the AAG/MPG glycosylase.

Authors:  Dragony Fu; Leona D Samson
Journal:  DNA Repair (Amst)       Date:  2011-11-11

3.  Crystal structures of 3-methyladenine DNA glycosylase MagIII and the recognition of alkylated bases.

Authors:  Brandt F Eichman; Eyleen J O'Rourke; J Pablo Radicella; Tom Ellenberger
Journal:  EMBO J       Date:  2003-10-01       Impact factor: 11.598

4.  Pre-steady-state kinetics shows differences in processing of various DNA lesions by Escherichia coli formamidopyrimidine-DNA glycosylase.

Authors:  Vladimir V Koval; Nikita A Kuznetsov; Dmitry O Zharkov; Alexander A Ishchenko; Kenneth T Douglas; Georgy A Nevinsky; Olga S Fedorova
Journal:  Nucleic Acids Res       Date:  2004-02-09       Impact factor: 16.971

5.  Protein tolerance to random amino acid change.

Authors:  Haiwei H Guo; Juno Choe; Lawrence A Loeb
Journal:  Proc Natl Acad Sci U S A       Date:  2004-06-14       Impact factor: 11.205

Review 6.  Overview of base excision repair biochemistry.

Authors:  Yun-Jeong Kim; David M Wilson
Journal:  Curr Mol Pharmacol       Date:  2012-01       Impact factor: 3.339

7.  Structure of Escherichia coli AlkA in complex with undamaged DNA.

Authors:  Brian R Bowman; Seongmin Lee; Shuyu Wang; Gregory L Verdine
Journal:  J Biol Chem       Date:  2010-09-15       Impact factor: 5.157

8.  Frameshift mutagenesis and microsatellite instability induced by human alkyladenine DNA glycosylase.

Authors:  Joanna Klapacz; Gondichatnahalli M Lingaraju; Haiwei H Guo; Dharini Shah; Ayelet Moar-Shoshani; Lawrence A Loeb; Leona D Samson
Journal:  Mol Cell       Date:  2010-03-26       Impact factor: 17.970

Review 9.  Regulation of DNA glycosylases and their role in limiting disease.

Authors:  Harini Sampath; Amanda K McCullough; R Stephen Lloyd
Journal:  Free Radic Res       Date:  2012-02-06

10.  Discrimination of lesion removal of N-methylpurine-DNA glycosylase revealed by a potent neutralizing monoclonal antibody.

Authors:  Sanjay Adhikari; Stephen J Kennel; Gargi Roy; Partha S Mitra; Sankar Mitra; Rabindra Roy
Journal:  DNA Repair (Amst)       Date:  2007-09-04
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