摘要
【目的】对玉米中长链酰基辅酶A合成酶1(ZmLACS1)基因及其蛋白磷酸化位点进行鉴定,为研究玉米脂肪酸的降解及其利用机制奠定基础。【方法】通过结构域分析查找质谱鉴定到蛋白中的长链酰基辅酶A合成酶1,通过系统发育树分析判断玉米中长链酰基辅酶A合成酶1与拟南芥超家族中长链酰基辅酶A合成酶的同源性,通过质谱分析鉴定该蛋白的磷酸化修饰位点。通过3D建模模拟长链酰基辅酶A合成酶1的结构以及磷酸化位点所在位置。【结果】玉米长链酰基辅酶A合成酶1(ZmLACS1)与拟南芥中的长链酰基辅酶A合成酶1(AtLACS1)具有高度同源性;通过质谱分析鉴定到3个该蛋白的磷酸化位点分别为S360、Y365和S366,同时鉴定到的磷酸化位点位于长链酰基辅酶A合成酶的保守结构域(AMP-binding domain)中,3个磷酸化位点位置一致,位于两个α螺旋中间,处于蛋白结构的关键位置。【结论】磷酸化修饰可能是调节长链酰基辅酶A合成酶1功能的关键性方式之一,ZmLACS1可能与AtLACS1在功能上具有相似性。
【Objective】This study identified the long chain acyl-CoA synthase 1 in Zea mays and detected its phosphorylation sites to provide basis for studying the mechanism of fatty acid degradation and utilization in Zea mays.【Method】Long chain acyl-CoA synthase 1 was detected by domain analysis and phylogenetic analysis was used to estimate its similarity with long chain acyl-CoA synthases in Arabidopsis superfamily.Mass spectrum was used to identify phosphorylation sites.The 3D structure of long chain acyl-CoA synthase 1 was modeled and the location of phosphorylation sites was confirmed.【Result】Long chain acyl-CoA synthase 1 in Zea mays and Arabidopsis thaliana was highly homologous.Phosphorylation sites of S360,Y365 and S366 were detected by mass spectrum and they were located in the conserved domain of long chain acyl-CoA synthase family(AMP-binding domain).The location of identified phosphorylation sites was consistent and they were in an important location between twoα-spirals.【Conclusion】Phosphorylation may be an important way for regulating the function of long chain acyl-CoA synthase 1 and it is speculated that it had similar function in Zea mays and Arabidopsis thaliana.
作者
陈莹
王晓峰
陈少林
CHEN Ying;WANG Xiaofeng;CHEN Shaolin(Biomass Energy Center for Arid and Semi-Arid Lands,College of Life Sciences,Northwest A&F University,Yangling,Shaanxi 712100,China)
出处
《西北农林科技大学学报（自然科学版）》
CSCD
北大核心
2020年第4期49-55,共7页
Journal of Northwest A&F University(Natural Science Edition)
基金
国家自然科学基金项目(31770207)
科技部“十二五”农村领域国家科技计划项目(2015BAD15B0503)。
