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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.
College of Life
Science Henan Normal University, Xinxiang 453007, ChinaCorresponding
author. Tel.: +86-373-332-3880; Fax: +86-373-332-6341; E-mail address:
dxdhy@163.com
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