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溶血磷脂酸酰基转移酶(LPAAT)是植物种子油脂合成的关键酶。本研究从花生(Arachis hypogaea L.)栽培品种花育32号和4个花生区组二倍体野生种中克隆得到编码LPAAT的基因序列。从花育32号获得的两条cDNA序列rlpaat-1和rlpaat-2开放阅读框均为1 131 bp,编码376个氨基酸,二者存在11个SNP差异位点,编码的氨基酸序列LPAAT-1和LPAAT-2有1个氨基酸残基的差异。LPAAT蛋白具有典型的酰基转移酶功能结构域以及4个保守氨基酸基序。之后从花育32号得到两条DNA序列,glpaat-1和glpaat-2长度分别为3 729 bp和3 736 bp,均由12个外显子和11个内含子组成,二者共存在37处碱基差异,其中34处为SNP位点。4个花生区组二倍体野生种各获得一条LPAAT序列,A.correntina,A.duranensis,A.batizocoi和A.ipaensis LPAAT的序列长度分别为3 757 bp、3 757 bp、3 742 bp和3 756 bp。核苷酸序列多态性和系统进化树分析表明,栽培品种LPAAT的两条序列glpaat-2与glpaat-1分别来自A、B染色体组。
Lysophosphatidylcholine acyltransferase (LPAAT) is a key enzyme in plant seed oil synthesis. In this study, the gene sequence encoding LPAAT was cloned from the diploid wild species of Arachis hypogaea L. cultivar Huayu 32 and 4 peanut groups. The two open reading frames (rlpaat-1 and rlpaat-2) of two cDNA sequences obtained from Huayu No.32 were 1 131 bp, encoding 376 amino acids. There were 11 SNP sites in the two sequences, encoding the amino acid sequence LPAAT-1 and LPAAT-2 has one amino acid residue difference. The LPAAT protein has a typical acyltransferase functional domain and four conserved amino acid motifs. Two DNA sequences were obtained from Huayu No.32. The lengths of glpaat-1 and glpaat-2 were 3 729 bp and 3 736 bp respectively, which consisted of 12 exons and 11 introns, both of which coexisted 37 There were 34 base pairs of SNPs. The sequences of LPAAT were obtained from 4 peanut diploid wild species respectively. The sequences of LPAAT from A. correntina, A.duranensis, A.batizocoi and A.ipaensis were 3 757 bp, 3 757 bp, 3 742 bp and 3 756 bp. The nucleotide sequence polymorphism and phylogenetic tree analysis showed that the two sequences of glpaat-2 and glpaat-1 of LPAAT were from A and B genomes respectively.