摘要
蔗糖合成酶(sucrose synthase,SS)作为催化蔗糖代谢的关键酶之一,能够参与蔗糖的代谢和运输,调节细胞分化与细胞壁的形成,对调控作物的品质和产量也有重要作用。克隆出菠萝蜜AhSS2基因并对其进行生物信息学分析。菠萝蜜AhSS2基因的开放阅读框(open reading frame,ORF)全长2436 bp,共编码811个氨基酸,其蛋白理化性质预测显示,相对分子量是92.583 ku,等电点pI为5.77,属亲水性酸性蛋白质,二级结构主要为Alpha helix(α-螺旋)。保守结构域分析显示,菠萝蜜AhSS2基因属于PLN00142超级家族成员,主要包括蔗糖合成酶结构域(Sucrose_synth)与糖基转移酶结构域(Glycos_transf_1)2个保守结构域。磷酸化位点预测显示,菠萝蜜AhSS2基因蛋白的磷酸化位点主要是丝氨酸(Ser)磷酸化位点。系统发育树分析显示,菠萝蜜AhSS2基因在分类上属SSⅡ。本研究为进一步研究菠萝蜜蔗糖合成酶家族成员的功能提供依据。
Sucrose synthase(SS)is one of the key enzymes catalyzing sucrose metabolism.It can participate in sucrose metabolism and transportation,regulate cell differentiation and cell wall formation,and also play an important role in regulating crop quality and yield.Jackfruit AhSS2 gene was cloned and bioinformatic analysis was performed.The open reading frame(ORF)of jackfruit AhSS2 gene is full-length 2436 bp,encoding a total of 811 amino acids.The predicted relative molecular weight of the protein is 92.583ku,and the isoelectric point(Pi)is 5.77.It is a hydrophilic acidic protein and its secondary structure is mainly alpha helix(α-Spiral).The conserved domain analysis showed that the jackfruit AhSS2 gene belonged to a PLN00142 superfamily member,including two conserved domains:sucrose synthase domain(Sucrose_synth)and glycosyltransferase domain(glycos_transf_1).Prediction of phosphorylation sites showed that the phosphorylation sites of the jackfruit AhSS2 gene are mainly serine(Ser)phosphorylation sites.Phylogenetic tree analysis showed that the jackfruit AhSS2 gene belonged to SSII in classification.This study provides a basis for further research on the function of jackfruit sucrose synthase family members.
作者
薛亚茹
李莹
李映志
XUE Yaru;LI Ying;LI Yingzhi(Coastal Agricultural College,Guangdong Ocean University,Zhanjiang,Guangdong 524000,China)
出处
《热带农业科学》
2021年第12期89-95,共7页
Chinese Journal of Tropical Agriculture
基金
广东海洋大学创新强校工程科研项目(No.GDOU2016050256,No.GDOU2013050319,No.GDOU2013050217)。
关键词
菠萝蜜
蔗糖合成酶
生物信息学
系统进化分析
jackfruit
sucrose synthase
bioinformatics analysis
phylogenetic analysis
