利用生物信息学方法对优势褐蛋鸡热休克蛋白90-aa1 (hsp90aa1)基因7 ~ 8号内含子进行了分析

Young I. Irivboje, A. Fafiolu, O. Irivboje, C. Ikeobi
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引用次数: 0

摘要

HSP90AA1是HSP90的一种异构体,已被鉴定为在基本细胞事件中起重要作用。它在鸡体内被激活以应对热应激。本研究旨在利用生物信息学工具对优势褐蛋鸡(DBL)和部分鸟类HSP90AA1基因的生化特征和结构特征进行计算分析,并对其进化关系进行研究。ProtParam的物理化学性质。翻译后修饰位点扫描prosite,磷酸化位点扫描Netphos-3.1,泛素化位点扫描BDM-PUB程序,二级结构扫描PDBSUM,用SWISS-model进行同源性建模。结果表明,DBL HSP90AA1蛋白的7号内含子和8号外显子分子量为24681.19Da,不稳定性指数为27.60,包含n-肉豆肉酰化、蛋白激酶- c -磷酸化和酪氨酸激酶-磷酸化位点-2个翻译后修饰位点、4-丝氨酸和2-苏氨酸磷酸化位点和12个泛素化位点。进化关系研究发现,日本鹌鹑与DBL和鸡属于姐妹分支。在鸟类中检测到的基序显示该基因高度保守。二级结构由16个螺旋,3个薄片和14股组成。与人类MC-HSP90-alpha序列同源性为87.25%。本研究阐明了热应激下DBL中HSP90AA1的组成及特征。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
Characterization of intron 7 to exon 8 of heat shock protein 90-aa1 (hsp90aa1) gene in dominant brown layer chicken using some bioinformatic tools
HSP90AA1, an isoform of HSP90 has been characterized to indicate it plays important roles in basic cellular events. It is activated in chicken in response to heat stress. This study was aimed at the computational analysis of the biochemical cum structural features and an evolutionary relationship study on the HSP90AA1 gene in Dominant brown layers (DBL) and some selected avian species using bioinformatics tools. ProtParam for physicochemical properties. Scanprosite for post-translational modification sites, Netphos-3.1 for phosphorylation sites, BDM-PUB program for Ubiquitination sites, PDBSUM for Secondary structure and homology modelling with SWISS-model. The findings revealed that intron 7 and exon 8 of HSP90AA1 protein in DBL had a molecular weight of 24681.19Da and an instability index of 27.60, contains N-myristoylation, Protein-kinase-C-phosphorylation and Tyrosine-kinase-phosphorylation site-2 post-translational modification sites, 4-serine and 2-threonine phosphorylation sites and 12-ubiquitination sites. The evolutionary relationship study found Japanese quail to be in a sister branch close to DBL and chicken. Motifs detected in the avian species revealed the gene to be highly conserved. The secondary structure consisted of 16-helices, 3-sheets and 14-strands. The homology modelling was 87.25% sequence identity with human MC-HSP90-alpha. The study elucidates the components and characteristics of HSP90AA1 in DBL in response to heat stress.
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