A model for 3-methyladenine recognition by 3-methyladenine DNA glycosylase I (TAG) from Staphylococcus aureus

Xiaofeng Zhu; Xuan Yan; Lester G. Carter; Huanting Liu; Shirley Graham; Peter J. Coote; James Naismith

doi:10.1107/S1744309112016363

A model for 3-methyladenine recognition by 3-methyladenine DNA glycosylase I (TAG) from Staphylococcus aureus

Xiaofeng Zhu, Xuan Yan, Lester G. Carter, Huanting Liu, Shirley Graham, Peter J. Coote, James Naismith

Research output: Contribution to journal › Article › peer-review

Abstract

The removal of chemically damaged DNA bases such as 3-methyladenine (3-MeA) is an essential process in all living organisms and is catalyzed by the enzyme 3-MeA DNA glycosylase I. A key question is how the enzyme selectively recognizes the alkylated 3-MeA over the much more abundant adenine. The crystal structures of native and Y16F-mutant 3-MeA DNA glycosylase I from Staphylococcus aureus in complex with 3-MeA are reported to 1.8 and 2.2 angstrom resolution, respectively. Isothermal titration calorimetry shows that protonation of 3-MeA decreases its binding affinity, confirming previous fluorescence studies that show that chargecharge recognition is not critical for the selection of 3-MeA over adenine. It is hypothesized that the hydrogen-bonding pattern of Glu38 and Tyr16 of 3-MeA DNA glycosylase I with a particular tautomer unique to 3-MeA contributes to recognition and selection.

Original language	English
Pages (from-to)	610-615
Number of pages	6
Journal	Acta Crystallographica. Section F, Structural biology and crystallization communications
Volume	68
DOIs	https://doi.org/10.1107/S1744309112016363
Publication status	Published - Jun 2012

Keywords

3-methyladenine DNA glycosylase I
Fluorescence measurements
ITC
DNA repair
Recognition

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10.1107/S1744309112016363

Zhu2012ActaCrystF 5204
Copyright © International Union of Crystallography.
Final published version, 796 KB

BBSRC BBS/B/14426: SPORT
Naismith, J. (PI)
BBSRC
18/10/04 → 30/04/12
Project: Standard

Cite this

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title = "A model for 3-methyladenine recognition by 3-methyladenine DNA glycosylase I (TAG) from Staphylococcus aureus",

abstract = "The removal of chemically damaged DNA bases such as 3-methyladenine (3-MeA) is an essential process in all living organisms and is catalyzed by the enzyme 3-MeA DNA glycosylase I. A key question is how the enzyme selectively recognizes the alkylated 3-MeA over the much more abundant adenine. The crystal structures of native and Y16F-mutant 3-MeA DNA glycosylase I from Staphylococcus aureus in complex with 3-MeA are reported to 1.8 and 2.2 angstrom resolution, respectively. Isothermal titration calorimetry shows that protonation of 3-MeA decreases its binding affinity, confirming previous fluorescence studies that show that chargecharge recognition is not critical for the selection of 3-MeA over adenine. It is hypothesized that the hydrogen-bonding pattern of Glu38 and Tyr16 of 3-MeA DNA glycosylase I with a particular tautomer unique to 3-MeA contributes to recognition and selection.",

keywords = "3-methyladenine DNA glycosylase I, Fluorescence measurements, ITC, DNA repair, Recognition",

author = "Xiaofeng Zhu and Xuan Yan and Carter, {Lester G.} and Huanting Liu and Shirley Graham and Coote, {Peter J.} and James Naismith",

year = "2012",

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doi = "10.1107/S1744309112016363",

language = "English",

volume = "68",

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T1 - A model for 3-methyladenine recognition by 3-methyladenine DNA glycosylase I (TAG) from Staphylococcus aureus

AU - Zhu, Xiaofeng

AU - Yan, Xuan

AU - Carter, Lester G.

AU - Liu, Huanting

AU - Graham, Shirley

AU - Coote, Peter J.

AU - Naismith, James

PY - 2012/6

Y1 - 2012/6

N2 - The removal of chemically damaged DNA bases such as 3-methyladenine (3-MeA) is an essential process in all living organisms and is catalyzed by the enzyme 3-MeA DNA glycosylase I. A key question is how the enzyme selectively recognizes the alkylated 3-MeA over the much more abundant adenine. The crystal structures of native and Y16F-mutant 3-MeA DNA glycosylase I from Staphylococcus aureus in complex with 3-MeA are reported to 1.8 and 2.2 angstrom resolution, respectively. Isothermal titration calorimetry shows that protonation of 3-MeA decreases its binding affinity, confirming previous fluorescence studies that show that chargecharge recognition is not critical for the selection of 3-MeA over adenine. It is hypothesized that the hydrogen-bonding pattern of Glu38 and Tyr16 of 3-MeA DNA glycosylase I with a particular tautomer unique to 3-MeA contributes to recognition and selection.

AB - The removal of chemically damaged DNA bases such as 3-methyladenine (3-MeA) is an essential process in all living organisms and is catalyzed by the enzyme 3-MeA DNA glycosylase I. A key question is how the enzyme selectively recognizes the alkylated 3-MeA over the much more abundant adenine. The crystal structures of native and Y16F-mutant 3-MeA DNA glycosylase I from Staphylococcus aureus in complex with 3-MeA are reported to 1.8 and 2.2 angstrom resolution, respectively. Isothermal titration calorimetry shows that protonation of 3-MeA decreases its binding affinity, confirming previous fluorescence studies that show that chargecharge recognition is not critical for the selection of 3-MeA over adenine. It is hypothesized that the hydrogen-bonding pattern of Glu38 and Tyr16 of 3-MeA DNA glycosylase I with a particular tautomer unique to 3-MeA contributes to recognition and selection.

KW - 3-methyladenine DNA glycosylase I

KW - Fluorescence measurements

KW - ITC

KW - DNA repair

KW - Recognition

U2 - 10.1107/S1744309112016363

DO - 10.1107/S1744309112016363

M3 - Article

SN - 1744-3091

VL - 68

SP - 610

EP - 615

JO - Acta Crystallographica. Section F, Structural biology and crystallization communications

JF - Acta Crystallographica. Section F, Structural biology and crystallization communications

ER -

A model for 3-methyladenine recognition by 3-methyladenine DNA glycosylase I (TAG) from Staphylococcus aureus

Abstract

Keywords

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Projects

BBSRC BBS/B/14426: SPORT

Cite this