Structural and functional characterization of annexin 1 from Medicago truncatula

被引:15
作者
Kodavali, Praveen Kumar [1 ]
Skowronek, Krzysztof [1 ]
Koszela-Piotrowska, Izabela [1 ]
Strzelecka-Kiliszek, Agnieszka [1 ]
Pawlowski, Krzysztof [2 ,3 ]
Pikula, Slawomir [1 ]
机构
[1] M Nencki Inst Expt Biol, Dept Biochem, PL-02093 Warsaw, Poland
[2] M Nencki Inst Expt Biol, Dept Mol & Cellular Neurobiol, PL-02093 Warsaw, Poland
[3] Warsaw Univ Life Sci, Fac Agr & Biol, Dept Expt Design & Bioinformat, PL-02787 Warsaw, Poland
关键词
Annexin; 1; Ion channel; Protein structure; Medicago truncatula; GOSSYPIUM-HIRSUTUM; CRYSTAL-STRUCTURE; PLANT ANNEXINS; STRESS; EXPRESSION; BINDING; PROTEIN; GENE; IDENTIFICATION; TOLERANCE;
D O I
10.1016/j.plaphy.2013.08.010
中图分类号
Q94 [植物学];
学科分类号
071001 ;
摘要
Annexins are calcium- and membrane-binding proteins that have been shown to have diverse properties such as actin, integrin and GTP binding, both in animals and plants. Recently, Medicago truncatula annexin 1 (AnnMt1) has been suggested to participate in nodulation (Nod factor signaling) and mycorrhization in legume plants. In this report we demonstrate for the first time that recombinant AnnMt1 (rec-AnnMt1) mediates membrane permeabilization to cations with conductance ranging from 16 pS to 329 pS. In agreement with other structurally determined annexins, homology modeling of AnnMt1 suggests that most of the functional determinants are found on the convex surface of the modeled structure. In conclusion, we propose a potential constitutive role of AnnMt1 in Nod factor signaling as a non-specific ion channel. (C) 2013 Elsevier Masson SAS. All rights reserved.
引用
收藏
页码:56 / 62
页数:7
相关论文
共 49 条
[1]   Matrix Mg2+ regulates mitochondrial ATP-dependent potassium channel from heart [J].
Bednarezyk, P ;
Dolowy, K ;
Szewczyk, A .
FEBS LETTERS, 2005, 579 (07) :1625-1632
[2]   The NFP locus of Medicago truncatula controls an early step of Nod factor signal transduction upstream of a rapid calcium flux and root hair deformation [J].
Ben Amor, B ;
Shaw, SL ;
Oldroyd, GED ;
Maillet, F ;
Penmetsa, RV ;
Cook, D ;
Long, SR ;
Dénarié, J ;
Gough, C .
PLANT JOURNAL, 2003, 34 (04) :495-506
[3]  
Breton G, 2000, PLANT CELL PHYSIOL, V41, P177, DOI 10.1093/pcp/41.2.177
[4]  
Cantero A., 2000, PLANT PHYSIOL BIOCH, V44, P13
[5]   Transcriptome profiling identified novel genes associated with aluminum toxicity, resistance and tolerance in Medicago truncatula [J].
Chandran, Divya ;
Sharopova, Natasha ;
Ivashuta, Sergey ;
Gantt, J. Stephen ;
VandenBosch, Kathryn A. ;
Samac, Deborah A. .
PLANTA, 2008, 228 (01) :151-166
[6]   Differential expression of members of the annexin multigene family in Arabidopsis [J].
Clark, GB ;
Sessions, A ;
Eastburn, DJ ;
Roux, SJ .
PLANT PHYSIOLOGY, 2001, 126 (03) :1072-1084
[7]   Evolutionary adaptation of plant annexins has diversified their molecular structures, interactions and functional roles [J].
Clark, Greg B. ;
Morgan, Reginald O. ;
Fernandez, Maria-Pilar ;
Roux, Stanley J. .
NEW PHYTOLOGIST, 2012, 196 (03) :695-712
[8]   Structural determinants for plant annexin-membrane interactions [J].
Dabitz, N ;
Hu, NJ ;
Yusof, AM ;
Tranter, N ;
Winter, A ;
Daley, M ;
Zschörnig, O ;
Brisson, A ;
Hofmann, A .
BIOCHEMISTRY, 2005, 44 (49) :16292-16300
[9]   The Nod factor-elicited annexin MtAnn1 is preferentially localised at the nuclear periphery in symbiotically activated root tissues of Medicago truncatula [J].
de Carvalho-Niebel, F ;
Timmers, ACJ ;
Chabaud, M ;
Defaux-Petras, A ;
Barker, DG .
PLANT JOURNAL, 2002, 32 (03) :343-352
[10]   Breaking the code: Ca2+ sensors in plant signalling [J].
DeFalco, Thomas A. ;
Bender, Kyle W. ;
Snedden, Wayne A. .
BIOCHEMICAL JOURNAL, 2010, 425 :27-40