Ectopic expression of ThCYP1, a stress-responsive cyclophilin gene from Thellungiella halophila, confers salt tolerance in fission yeast and tobacco cells

被引:56
作者
Chen, An-Ping
Wang, Gui-Ling
Qu, Zhan-Liang
Lu, Chun-Xia
Liu, Ning
Wang, Fang
Xia, Gui-Xian [1 ]
机构
[1] Chinese Acad Sci, Natl Key Lab Plant Genom, Inst Microbiol, Beijing 100080, Peoples R China
[2] Chinese Acad Sci, Grad Sch, Beijing 100049, Peoples R China
[3] Hebei Univ, Coll Life Sci, Baoding 071002, Peoples R China
基金
中国国家自然科学基金;
关键词
cyclophilin; fission yeast; salt tolerance; Thellungiella halophila; tobacco BY-2 cell;
D O I
10.1007/s00299-006-0238-y
中图分类号
Q94 [植物学];
学科分类号
071001 ;
摘要
The halophyte Thellungiella halophila (salt cress) is an ideal model system for studying the molecular mechanisms of salinity tolerance in plants. Herein, we report the identification of a stress-responsive cyclophilin gene (ThCYP1) from T. halophila, using fission yeast as a functional system. The expression of ThCYP1 is highly inducible by salt, abscisic acid (ABA), H2O2 and heat shock. Ectopic overexpression of the ThCYP1 gene enhance the salt tolerance capacity of fission yeast and tobacco (Nicotiana tabacum L.) cv. Bright Yellow 2 (BY-2) cells significantly. ThCYP1 is expressed constitutively in roots, stems, leaves and flowers, with higher expression occurring in the roots and flowers. The ThCYP1 proteins are distributed widely within the cell, but are enriched significantly in the nucleus. The present results suggest that ThCYP1 may participate in response to stresses in the salt cress, perhaps by regulating appropriate folding of certain stress-related proteins, or in the signal transduction processes.
引用
收藏
页码:237 / 245
页数:9
相关论文
共 45 条
[1]  
Alfa C., 1993, EXPT FISSION YEAST L
[2]   HIGH-EFFICIENCY TRANSFORMATION OF CULTURED TOBACCO CELLS [J].
AN, GH .
PLANT PHYSIOLOGY, 1985, 79 (02) :568-570
[3]   Regulation of vegetative phase change in Arabidopsis thaliana by cyclophilin 40 [J].
Berardini, TZ ;
Bollman, K ;
Sun, H ;
Poethig, RS .
SCIENCE, 2001, 291 (5512) :2405-2407
[4]   CONSIDERATION OF POSSIBILITY THAT SLOW STEP IN PROTEIN DENATURATION REACTIONS IS DUE TO CIS-TRANS ISOMERISM OF PROLINE RESIDUES [J].
BRANDTS, JF ;
HALVORSON, HR ;
BRENNAN, M .
BIOCHEMISTRY, 1975, 14 (22) :4953-4963
[5]   Regulation of the tyrosine kinase Itk by the peptidyl-prolyl isomerase cyclophilin A [J].
Brazin, KN ;
Mallis, RJ ;
Fulton, DB ;
Andreotti, AH .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2002, 99 (04) :1899-1904
[7]   Characterization of the cyclophilin gene family of Arabidopsis thaliana and phylogenetic analysis of known cyclophilin proteins [J].
Chou, IT ;
Gasser, CS .
PLANT MOLECULAR BIOLOGY, 1997, 35 (06) :873-892
[8]   Activation of a phytopathogenic bacterial effector protein by a eukaryotic cyclophilin [J].
Coaker, G ;
Falick, A ;
Staskawicz, B .
SCIENCE, 2005, 308 (5721) :548-550
[9]   Agrobacterium VirDa protein interacts with plant host cyclophilins [J].
Deng, WY ;
Chen, LS ;
Wood, DW ;
Metcalfe, T ;
Liang, XY ;
Gordon, MP ;
Comai, L ;
Nester, EW .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1998, 95 (12) :7040-7045
[10]   An Arabidopsis immunophilin, AtFKBP12, binds to AtFIP37 (FKBP interacting protein) in an interaction that is disrupted by FK506 [J].
Faure, JD ;
Gingerich, D ;
Howell, SH .
PLANT JOURNAL, 1998, 15 (06) :783-789