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作 者:曾艳玲[1] 谭晓风[1] 蒋瑶[1] 刘敏[1] 王建勇[1] 周俊琴[1]
机构地区:[1]中南林业科技大学森林培养与保护教育部重点实验室经济林育种与栽培国家林业局重点实验室,长沙410004
出 处:《林业科学》2013年第11期164-170,共7页Scientia Silvae Sinicae
基 金:国家自然科学基金项目(31070603);中南林业科技大学青年基金重点项目(QJ2011008A)
摘 要:果糖-1,6-二磷酸醛缩酶(fructose-1,6-diphosphatealdolase,FBA,EC4.1.2.13),简称醛缩酶,是糖酵解代谢途径中第4步关键酶,催化果糖-1,6-二磷酸(Fru.1,6-BP)可逆地裂解为磷酸二羟丙酮(DHAP)和3-磷酸甘油醛(G.3-P)(Rutter,1964)。Fructose-1,6-diphosphate aldolase (FBA) in plants is not only one of the key regulatory enzyme in glycolysis pathway but also provide substrate source for two key components of oil synthesis. In this paper, a new FBA full-length cDNA of Camellia oleifera seed was isolated and cloned by RACE technology, and was named CoFBA4 (GenBank number: JX914590). CoFBA4 had an open reading frame with ! 185 base pairs encoding 394 amino acids. Sequence analysis showed that CoFBA4 had nearest genetic distance with FBA of Arabidopsis thaliana, and belonged to subfamily A. CoFBA4 contained glycosylation and fructose-1,6-diphosphate aldolase activity site, but had no transmembrane domain. CoFBA4 belonged to hydrophilic protein. Subcellular localization analysis showed that CoFBA4 acted out of cell. There was a positive relationship between expression abundance of CoFBA4 gene and oil yield from different superior clones during the same maturity period.
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