Purification, crystallization and preliminary X-ray diffraction analysis of the Whirly domain of StWhy2 in complex with single-stranded DNA

被引：4

作者：

Cappadocia, Laurent ^{[1
]}

Sygusch, Jurgen ^{[1
]}

Brisson, Normand ^{[1
]}

机构：

[1] Univ Montreal, Dept Biochem, Stn Ctr Ville, Montreal, PQ H3C 3J7, Canada

来源：

ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS | 2008年 / 64卷

基金：

加拿大健康研究院; 加拿大自然科学与工程研究理事会;

关键词：

D O I：

10.1107/S1744309108032399

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

StWhy1 and StWhy2 are members of the Whirly family of single-stranded DNA (ssDNA) binding proteins. To understand the mode of binding of the Whirly proteins to single-stranded DNA, crystals of the Whirly domains of both StWhy1 and StWhy2 in complex with single-stranded DNA were obtained by the hanging-drop vapour-diffusion method. The diffraction patterns of the StWhy1-ssDNA complex crystals displayed severe anisotropy and were of low resolution, making them unsuitable for structure determination. In contrast, the crystals of the StWhy2-ssDNA complex diffracted isotropically to 2.20 angstrom resolution. The crystallization and data collection to 2.20 angstrom resolution of StWhy2 in the free form are also reported.

引用

页码：1056 / 1059

页数：4

共 9 条

[1] A "whirly" transcription factor is required for salicylic acid-dependent disease resistance in Arabidopsis [J].

Desveaux, D ;

Subramaniam, R ;

Després, C ;

Mess, JN ;

Lévesque, C ;

Fobert, PR ;

Dangl, JL ;

Brisson, N .

DEVELOPMENTAL CELL, 2004, 6 (02) :229-240

[2] Crystallization and preliminary X-ray crystallographic analysis of p24, a component of the potato nuclear factor PBF-2 [J].

Desveaux, D ;

Allard, J ;

Brisson, N ;

Sygusch, J .

ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY, 2002, 58 :296-298

[3] PBF-2 is a novel single-stranded DNA binding factor implicated in PR-10a gene activation in potato [J].

Desveaux, D ;

Després, C ;

Joyeux, A ;

Subramaniam, R ;

Brisson, N .

PLANT CELL, 2000, 12 (08) :1477-1489

[4] A new family of plant transcription factors displays a novel ssDNA-binding surface [J].

Desveaux, D ;

Allard, J ;

Brisson, N ;

Sygusch, J .

NATURE STRUCTURAL BIOLOGY, 2002, 9 (07) :512-517

[5] A deliberate approach to screening for initial crystallization conditions of biological macromolecules [J].

Luft, JR ;

Collins, RJ ;

Fehrman, NA ;

Lauricella, AM ;

Veatch, CK ;

DeTitta, GT .

JOURNAL OF STRUCTURAL BIOLOGY, 2003, 142 (01) :170-179

[6] Overexpression of mtDNA-associated AtWhy2 compromises mitochondrial function [J].

Marechal, Alexandre ;

Parent, Jean-Sebastien ;

Sabar, Mohammed ;

Veronneau-Lafortune, Felix ;

Abou-Rached, Charbel ;

Brisson, Normand .

BMC PLANT BIOLOGY, 2008, 8 (1)

[7] Processing of X-ray diffraction data collected in oscillation mode [J].

Otwinowski, Z ;

Minor, W .

MACROMOLECULAR CRYSTALLOGRAPHY, PT A, 1997, 276 :307-326

[8] A family of RRM-type RNA-binding proteins specific to plant mitochondria [J].

Vermel, M ;

Guermann, B ;

Delage, L ;

Grienenberger, JM ;

Maréchal-Drouard, L ;

Gualberto, JM .

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2002, 99 (09) :5866-5871

[9] Single-stranded DNA binding factor AtWHY1 modulates telomere length homeostasis in Arabidopsis [J].

Yoo, Hyun Hee ;

Kwon, Chian ;

Lee, Myeong Min ;

Chung, In Kwon .

PLANT JOURNAL, 2007, 49 (03) :442-451

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