高粱苯丙氨酸解氨酶(SbPAL)编码蛋白的生物信息学分析

Bioinformatics Analysis of Phenylalanine Ammonia-lyase(SbPAL)Protein-coding in Sorghum

高粱是世界上一种重要的粮食作物,具有耐寒耐高温等优良性质,挖掘高粱抗病基因(如PAL),在基因水平上进行遗传改良,提高高粱对贫瘠土地的耐受性仍是研究热点之一。以高粱的苯丙氨酸解氨酶基因(SbPAL)为研究对象,运用生物信息学方法对其编码蛋白的结构、理化性质及功能结构域进行分析,以期揭示苯丙解氨酶的基本信息。结果表明,高粱SbPAL基因的编码序列(Coding sequences,CDS)全长为2 145 bp,编码714个氨基酸;高粱SbPAL蛋白主要位于细胞基质中,二级结构以无规则卷曲和α-螺旋为主,三级结构预测其为同源四聚体结构,由4个相同亚基对称性组成,各亚基之间由配体DTT共价连接。多序列比对结果表明,高粱SbPAL蛋白与拟南芥、水稻、葡萄、烟草等蛋白的同源性较高,为83.31%,SbPAL基因与玉米、水稻和大麦有着较近的亲缘关系,PAL在这些作物中主要参与木质素和植保素的合成。此分析结果将为后续进一步研究SbPAL对木质素、植保素等合成的分子机制与抗病性关系奠定一定的理论基础。

Sorghum is an important food crop in the world, it can resist cold as well as hot temperature and has other excellent properties. Mining resistance genes （such as PAL ） and geneticly modifying it at the gene level in sorghum to improve its tolerance of sorghum on marginal land is still one of the hot topics in research field. In this paper, sorghum phenylalanine ammonia-lyase gene （SbPAL） was seen as the subject and was studied by using the method of bioinformatics to analyze its structure of the encoded protein, physicochemical properties and functional domains, to reveal the basic information of phenylalanyl ammonia-lyase. The results showed that coding sequence of sorghum SbPAL gene （CDS） had a total length of 2 145 bp, encoding 714 amino acids. Sorghum SbPAL protein was mainly located in the extracellular matrix. Its secondary structure concluded random coil and α-helix and the three-dimensional structure which had a homologous tetramer. Four identical subunits made up the symmetry structure which was connected by covalent ligands DTT between two subunits. The multiple sequence alignment results showed that they had a closer relationship between sorghum SbPAL and other protein of various species, such as A rabidopsis, rice, grapes, tobacco, and high homology whose value was 83.31%. The SbPAL gene shared closer relationship between maize, rice and barley in which PAL was mainly involved in the synthesis of lignin and phytoalexin. The result of this analysis will lay a theoretical foundation for further study of the molecular mechanisms of SbPAL involving in synthese of lignin and phytoalexins related to disease resistance.