Overexpression of suadea salsa S-adenosylmethionine synthetase gene promotes salt tolerance in transgenic tobacco

被引:63
作者
Qi, Yuan-Cheng [1 ,2 ]
Wang, Fei-Fei [1 ]
Zhang, Hui [3 ]
Liu, Wei-Qun [1 ]
机构
[1] Henan Agr Univ, Coll Life Sci, Zhengzhou 450002, Peoples R China
[2] Henan Agr Univ, Coll Tobacco Sci, Zhengzhou 450002, Peoples R China
[3] Shandong Normal Univ, Coll Life Sci, Key Lab Plant Stress Res, Jinan 250014, Peoples R China
关键词
Salt stress; Polyamines; S-adenosylmethionine synthetase; Transgenic tobacco; L-METHIONINE SYNTHETASE; ARGININE DECARBOXYLASE; DIFFERENTIAL ACCUMULATION; ARABIDOPSIS-THALIANA; ANTIOXIDANT ENZYMES; BRASSICA-JUNCEA; SUAEDA-SALSA; POLYAMINES; EXPRESSION; PLANTS;
D O I
10.1007/s11738-009-0403-3
中图分类号
Q94 [植物学];
学科分类号
071001 ;
摘要
The suadea salsa full-length S-adenosylmethionine synthetase (SsSAMS2) was introduced into tobacco (Nicotiana tabacum L.) by Agrobacterium tumefaciens-mediated transformation. The gene transformation and expression in tobacco were confirmed by PCR, RT-PCR and Northern blotting analysis. Several transgenic lines (ST lines) overexpressing SsSAMS2 gene under the control of cauliflower mosaic virus 35S promoter showed more seeds number and weight, and accumulated higher free total polyamines (PAs) than wild-type plants (WT lines) and transformants with blank vector (BT lines). Salt stress-induced damage was attenuated in these transgenic plants, in the symptom of maintaining higher photosynthetic rate and biomass. These results that the transgenic plants overexpressing suadea salsa SAMS2 are more tolerant to salt stress than wild-type plants suggest that PAs may play an important role in contributing salt tolerance to plants.
引用
收藏
页码:263 / 269
页数:7
相关论文
共 42 条
[1]   Biosynthesis, oxidation and conjugation of aliphatic polyamines in higher plants [J].
Bagni, N ;
Tassoni, A .
AMINO ACIDS, 2001, 20 (03) :301-317
[2]   POLYAMINES IN VARIOUS RICE (ORYZA-SATIVA) GENOTYPES WITH RESPECT TO SODIUM-CHLORIDE SALINITY [J].
BASU, R ;
GHOSH, B .
PHYSIOLOGIA PLANTARUM, 1991, 82 (04) :575-581
[3]   ANALYSIS OF A CDNA-ENCODING ARGININE DECARBOXYLASE FROM OAT REVEALS SIMILARITY TO THE ESCHERICHIA-COLI ARGININE DECARBOXYLASE AND EVIDENCE OF PROTEIN PROCESSING [J].
BELL, E ;
MALMBERG, RL .
MOLECULAR & GENERAL GENETICS, 1990, 224 (03) :431-436
[4]   PLANT PRODUCTIVITY AND ENVIRONMENT [J].
BOYER, JS .
SCIENCE, 1982, 218 (4571) :443-448
[5]  
CANTONI GL, 1953, J BIOL CHEM, V204, P403
[6]   S-adenosylmethionine and methylation [J].
Chiang, PK ;
Gordon, RK ;
Tal, J ;
Zeng, GC ;
Doctor, BP ;
Pardhasaradhi, K ;
McCann, PP .
FASEB JOURNAL, 1996, 10 (04) :471-480
[7]  
DEKEYSER RA, 1990, PLANT CELL, V2, P591, DOI 10.1105/tpc.2.7.591
[8]  
Doyle JJ., 1987, FOCUS, V19, P11, DOI DOI 10.2307/2419362
[9]   Photosynthesis in two wheat cultivars differing in salt susceptibility [J].
El-Shintinawy, F .
PHOTOSYNTHETICA, 2000, 38 (04) :615-620
[10]   SALINE CULTURE OF CROPS - A GENETIC APPROACH [J].
EPSTEIN, E ;
NORLYN, JD ;
RUSH, DW ;
KINGSBURY, RW ;
KELLEY, DB ;
CUNNINGHAM, GA ;
WRONA, AF .
SCIENCE, 1980, 210 (4468) :399-404