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Identification and Characterization of a Multigene Family Encoding Germin-Like Proteins in Cultivated Peanut (Arachis hypogaea L.)

文献类型： 外文期刊

作者： Chen, Xiaoping 4 ; Wang, Ming Li 3 ; Holbrook, Corley 2 ; Culbreath, Albert 5 ; Liang, Xuanqiang 4 ; Brenneman, Tim 5 ;

作者机构： 1.ARS, USDA, Crop Protect & Management Res Unit, Tifton, GA 31793 USA

2.ARS, USDA, Crop Genet & Breeding Res Unit, Tifton, GA 31793 USA

3.ARS, USDA, Plant Genet Resources Conservat Unit, Tifton, GA 31793 USA

4.Guangdong Acad Agr Sci, Crops Res Inst, Guangzhou, Guangdong, Peoples R China

5.Univ Georgia, Dept Plant Pathol, Tifton, GA 31793 USA

关键词： manganese: 7439-96-5;hydrogen peroxide: 7722-84-1;superoxide dismutase: 9054-89-1;EC 1.15.1.1;amino acid;expressed sequence tag;paraquat: 4685-14-7;pesticide;herbicide;oxalate oxidase: 9031-79-2;EC 1.2.3.4;reactive oxygen metabolites;germin-like protein 1: GLP1 protein;expression;germin-like protein 2: GLP-2;expression;oxidative damage;GenBank sequence data;enzyme activity

期刊名称：PLANT MOLECULAR BIOLOGY REPORTER （ 影响因子：1.595； 五年影响因子：2.042 ）

ISSN：

年卷期：

页码：

收录情况： SCI

摘要： Germin-like proteins (GLPs) play diversified roles in plant development and defense response. Here, we identified 36 expressed sequence tags (ESTs) encoding GLPs from peanut (Arachis hypogaea L.). After assembly, these ESTs were integrated into eight unigenes named AhGLP1 to AhGLP8, of which, three (AhGLP1-3) were comprised 14, ten, and seven EST clones, respectively, whereas the remaining ones were associated with one single clone. The length of the deduced amino acid (AA) residues ranged from 208 to 223 AAs except for AhGLP6 and AhGLP8, which were incomplete at the carboxyl terminus. All of the AhGLPs contained a possible N-terminal signal peptide that was 17 to 24 residues in length excluding AhGLP7, where there is likely a non-cleavable amino terminus. Phylogenetic analysis showed that these AhGLPs were classified into three subfamilies. Southern blot analysis indicated that AhGLP1 and AhGLP2 likely have multiple copies in the peanut genome. The recombinant mature AhGLP1 and AhGLP2 proteins were successfully expressed in Escherichia coli. The purified AhGLP2 has superoxide dismutase (SOD) activity in enzymatic assay, but not oxalate oxidase activity. The SOD activity of AhGLP2 was stable up to 70A degrees C and resistant to hydrogen peroxide, suggesting that AhGLP2 might be a manganese-containing SOD. Furthermore, AhGLP2 could confer E. coli resistance to oxidative damage caused by paraquat, suggesting that the AhGLP2 likely protects peanut plants from reactive oxygen metabolites. Thus, information provided in this study indicates the diverse nature of the peanut GLP family and suggests that some of AhGLPs might be involved in plant defense response.

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