The structure of the Arabidopsis thaliana SOS3:: Molecular mechanism of sensing calcium for salt stress response

被引:136
作者
Sánchez-Barrena, MJ
Martínez-Ripoll, M
Zhu, JK
Albert, A
机构
[1] CSIC, Inst Quim Fis Rocasolano, Grp Cristalog Macromol & Biol Estructural, E-28006 Madrid, Spain
[2] Univ Calif Riverside, Dept Bot & Plant Sci, Riverside, CA 92521 USA
[3] Univ Calif Riverside, Inst Integrat Genome Biol, Riverside, CA 92521 USA
关键词
calcium signaling; protein structure; salt tolerance; crystallography; EF-hand;
D O I
10.1016/j.jmb.2004.11.025
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The Arabidopsis thaliana SOS3 gene encodes a calcium sensor that is required for plant salt tolerance. The SOS3 protein binds to and activates the self-inhibited SOS2 protein kinase, which mediates the expression and activities of various transporters important for ion homeostasis under salt stress. SOS3 belongs to a unique family of calcium-binding proteins that contain two pairs of EF hand motifs with four putative metal-binding sites. We report the crystal structure of a dimeric SOS3 protein in complex with calcium, and with calcium and manganese. Analytical ultracentrifugation experiments and circular dichroism measurements show that calcium binding is responsible for the dimerization of SOS3. This leads to a change in the global shape and surface properties of the protein that may be sufficient to transmit the Ca2+ signal elicited during salt stress. (C) 2004 Elsevier Ltd. All rights reserved.
引用
收藏
页码:1253 / 1264
页数:12
相关论文
共 57 条
[1]   Methods used in the structure determination of bovine mitochondrial F-1 ATPase [J].
Abrahams, JP ;
Leslie, AGW .
ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY, 1996, 52 :30-42
[2]   BASIC LOCAL ALIGNMENT SEARCH TOOL [J].
ALTSCHUL, SF ;
GISH, W ;
MILLER, W ;
MYERS, EW ;
LIPMAN, DJ .
JOURNAL OF MOLECULAR BIOLOGY, 1990, 215 (03) :403-410
[3]   The protein content in crystals and packing coefficients in different space groups [J].
Andersson, KM ;
Hovmöller, S .
ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY, 2000, 56 :789-790
[4]   THE CCP4 SUITE - PROGRAMS FOR PROTEIN CRYSTALLOGRAPHY [J].
BAILEY, S .
ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY, 1994, 50 :760-763
[5]   Immunocytochemical localization and crystal structure of human frequenin (neuronal calcium sensor 1) [J].
Bourne, Y ;
Dannenberg, J ;
Pollmann, V ;
Marchot, P ;
Pongs, O .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2001, 276 (15) :11949-11955
[6]  
Brunger AT, 1998, ACTA CRYSTALLOGR D, V54, P905, DOI 10.1107/s0907444998003254
[7]   Miscellaneous algorithms for density modification [J].
Cowtan, K ;
Main, P .
ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY, 1998, 54 :487-493
[8]   REGULATORY SUBUNIT (CNB1 GENE-PRODUCT) OF YEAST CA2+/CALMODULIN-DEPENDENT PHOSPHOPROTEIN PHOSPHATASES IS REQUIRED FOR ADAPTATION TO PHEROMONE [J].
CYERT, MS ;
THORNER, J .
MOLECULAR AND CELLULAR BIOLOGY, 1992, 12 (08) :3460-3469
[9]   Maximum-likelihood heavy-atom parameter refinement for multiple isomorphous replacement and multiwavelength anomalous diffraction methods [J].
delaFortelle, E ;
Bricogne, G .
MACROMOLECULAR CRYSTALLOGRAPHY, PT A, 1997, 276 :472-494
[10]   COMPARISON OF THE ZINC-BINDING DOMAINS IN THE 7S NERVE GROWTH-FACTOR AND THE ZINC INSULIN HEXAMER [J].
DUNN, MF ;
PATTISON, SE ;
STORM, MC ;
QUIEL, E .
BIOCHEMISTRY, 1980, 19 (04) :718-725