Molecular cloning and analysis of a cDNA coding for chorismate synthase from the higher plant Corydalis sempervirens Pers.
Molecular cloning and analysis of a cDNA coding for chorismate synthase from the higher plant Corydalis sempervirens Pers.
复制标题
DOI：
10.1016/s0021-9258(18)54657-3
复制
发表时间：
1991-11
期刊：
影响因子：
--
通讯作者：
Andreas Schaller;J. Schmid;U. Leibinger;N. Amrhein
中科院分区：
文献类型：
--
作者：
Andreas Schaller;J. Schmid;U. Leibinger;N. Amrhein
氯酸合成酶催化微生物和植物中三种芳香族氨基酸生物合成的最后一步。我们已经从高等植物延胡索中克隆了该酶的cDNA。这是第一个从真核生物中获得的分支酸合成酶基因。测定了该基因的核苷酸序列，并用纯化的分支酸合成酶获得的胰蛋白酶多肽的氨基酸序列证实了该基因的同源性。与这两个已知细菌序列的同源性约为48%。该基因含有1341个碱基对的开放阅读框，编码447个氨基酸的蛋白质。这种分子质量为48,100道尔顿的蛋白质类似于叶绿体进口目标的分支酸合成酶前体。在分支酸合成酶mRNAs中观察到多个位置的多聚腺苷。
Chorismate synthase catalyzes the last common step in the biosynthesis of the three aromatic amino acids in microorganisms and plants. We have cloned a cDNA for this enzyme from the higher plant Corydalis sempervirens. This is the first chorismate synthase cDNA from a eukaryotic organism. The nucleotide sequence was determined and the identity of the cDNA was confirmed by the amino acid sequence of tryptic peptides obtained from purified chorismate synthase. The homology to the two known bacterial sequences is about 48%. The cDNA contains an open reading frame of 1341 base pairs, encoding a protein of 447 amino acids. This protein with a molecular mass of 48,100 daltons resembles a chorismate synthase precursor targeted for chloroplast import. Multiple sites of polyadenylation were observed in chorismate synthase mRNAs.