大白菜氨基醇磷酸转移酶cDNA AAPT3基因的克隆与表达

K. Kim, Jong Ho Park, S. Cho
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引用次数: 1

摘要

氨基醇磷酸转移酶催化二酰基甘油加CDP -氨基醇(如CDP -胆碱或CDP -乙醇胺)合成磷脂酰胆碱和磷脂酰乙醇胺。在此之前,我们认为该酶可能存在于白菜根中,现在我们报道了编码第三种氨基醇磷酸转移酶(AAPT3)异构体的AAPT3的cDNA克隆和表达分析。AAPT3包含一个1176 bp的开放阅读框,编码392个氨基酸的蛋白。在推导出的氨基酸水平上,它与大白菜AAPT1和AAPT2的同源性分别为96%和95%。逆转录聚合酶链反应结果表明,低温上调了AAPT3的表达,也上调了AAPT1和AAPT2的表达。
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Cloning and expression of a cDNA AAPT3 encoding aminoalcoholphosphotransferase Isoform from Chinese Cabbage
Aminoalcoholphosphotransferase catalyzes the synthesis of phosphatidylcholine and phosphatidylethanolamine from diacylglycerol plus a CDP‐aminoalcohol such as CDP‐choline or CDP‐ethanolamine. Previously we suggested the presence of possible isoforms of this enzyme from Chinese cabbage roots and now report the cDNA cloning and expression analysis of AAPT3 encoding a third isoform of aminoalcoholphosphotransferase (AAPT3). AAPT3 contains an open reading frame of 1,176 bp coding for a protein of 392 amino acids. It shares 96 and 95% identity with Chinese cabbage AAPT1 and AAPT2, respectively, at the deduced amino acid level. The results from reverse transcriptase‐polymerase chain reaction analysis indicate that expression of AAPT3 is up‐regulated by low temperature as well as AAPT1 and AAPT2.
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