Paper Details

PJB-2011-275

CLONING AND BIOINFORMATICS ANALYSIS OF ASPARTATE AMINOTRANSFERASE GENE IN ARABIDOPSIS THALIANA

HONGYING DUAN, XIAOSHENG DING, YONGANG YU, ZHIQIANG DUAN, YUNLONG HE, ZHIKUN DUAN AND YANQING ZHOU
Abstract


In this study, gene encoding Aspartate aminotransferase was cloned from Arabidopsis thaliana by RT-PCR, named F23N and its bioinformatics analysis was performed. It was found that there is one pyridoxal-phosphate attachment site at 250-270 (SYAKnmGLyGERIG) and other domains, furthermore, the transmembrane helices was not found in F23N, suggesting that F23N encoding product might not belong to membrane-protein. Combined with other Aspartate aminotransferase in Arabidopsis thaliana, they have obvious similarities, F23N and ASP4 take on 96% positives to each other, especially the similarity between F23N and Aspartate aminotransferase (BAE99790) reached 100%. In addition, the conserved genes encoding Aspartate aminotransferase from various species were analyzed by DNAMAN and found that F23N shows obvious comparability with those from some species in Dicotyledons and Monocotyledons. Furthermore, in the phylogenetic tree, these species analyzed were divided into two branches, one branch was composed of Protist, Eukaryotes, the other consist of Pan troglodytes and Tribolium castaneum, and Eukaryotes was further divided into two branches, which is mostly consistent with biological system.

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