Cold Shock Domain Proteins Affect Seed Germination and Growth of Arabidopsis thaliana Under Abiotic Stress Conditions

被引:89
|
作者
Park, Su Jung
Kwak, Kyung Jin
Oh, Tae Rin
Kim, Yeon Ok
Kang, Hunseung [1 ]
机构
[1] Chonnam Natl Univ, Coll Agr & Life Sci, Dept Plant Biotechnol, Agr Plant Stress Res Ctr, Kwangju 500757, South Korea
关键词
Abiotic stress; Arabidopsis thaliana; Cold shock domain protein; Cold shock protein; RNA chaperone; RNA-BINDING PROTEIN; ESCHERICHIA-COLI; FUNCTIONAL-CHARACTERIZATION; ADAPTATION PROCESS; HIGH SALINITY; CSPA-FAMILY; PLANTS; CONSERVATION; RESPONSES; CHAPERONE;
D O I
10.1093/pcp/pcp037
中图分类号
Q94 [植物学];
学科分类号
071001 ;
摘要
Unlike the well-known functions of cold shock proteins in prokaryotes during cold adaptation, the biological functions of cold shock domain proteins (CSDPs) in plants remain largely unknown. Here, we examined the functional roles of two structurally different CSDPs, CSDP1 harboring a long C-terminal glycine-rich region interspersed with seven CCHC-type zinc fingers and CSDP2 containing a far shorter glycine-rich region interspersed with two CCHC-type zinc fingers, in Arabidopsis thaliana under stress conditions. CSDP1 overexpression delayed the seed germination of Arabidopsis under dehydration or salt stress conditions, whereas CSDP2 overexpression accelerated the seed germination of Arabidopsis under salt stress conditions. CSDP1 and CSDP2 rescued the cold-sensitive glycine-rich RNA-binding protein 7 mutant plants from freezing damage to a different degree, and this rescuing capability was correlated with their ability to complement the cold-sensitive Escherichia coli BX04 mutant at low temperatures. The nucleic acid-binding properties of CSDPs varied depending on the N-terminal cold shock domain and the C-terminal glycine-rich zinc finger region. Collectively, these results showed that CSDP1 and CSDP2 perform different functions in seed germination and growth of Arabidopsis under stress conditions, and that the glycine-rich region interspersed with CCHC-type zinc fingers is particularly important for its nucleic acid-binding activities and function.
引用
收藏
页码:869 / 878
页数:10
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