Cloning and Sequence Analysis of a Lysophosphatidic Acid Acyltransferase Gene (LPAAT) in Arachis hypogaea L.and Wild Diploid Species
Lysophosphatidic acid acyltransferase (LPAAT) is a pivotal enzyme responsible for the acylation of lysophosphatidic acid (LPA) into phosphatidic acid (PA).In this study,we obtained the sequences of its encoding gene LPAAT from one cultivated variety and four wild diploid species.Two cDNA sequences rlpaat-1 and rlpaat-2 were isolated from Huayu32 and they both had an ORF (open reading frame) of 1 131 bp which encodes a putative protein of 376 amino acid residues.There were 11 different SNP (single nucleotide polymorphism) sites within rlpaat-1 and rlpaat-2,leading to one amino acid difference in the corresponding amino acid sequences LPAAT-1 and LPAAT-2.LPAAT protein comprised a conserved acyltransferase domain and four conserved motifs that existed in the whole acyltransferase family.Then DNA sequences were cloned from Huayu32 and four wild species.The length of glpaat-1 and glpaat-2 obtained from Huayu32 were 3 729 bp and 3 736 bp,respectively.Sequence alignment revealed that between glpaat-1 and glpaat-2,there were 37 different sites in total,of which 34 were SNP sites.But they both had 12 exons and 11 introns.One sequence was obtained from each wild species,for A.correntina,A.duranensis,A.batizocoi,A.ipaensis,the sequence length ofLPAA T was 3 757 bp,3 757 bp,3 742 bp and 3 756 bp,respectively.Nucleotide polymorphism analysis and phylogenetic analysis indicated that glpaat-1 and glpaat-2 came from different genomes.
NETL
NSTL
万方数据
维普
