意大利蜜蜂DnaJC28的生物信息学分析

Bioinformatics Analysis of DnaJC28 in Apis Mellifera

DnaJ家族基因在动植物热激胁迫响应过程发挥重要作用。前期,我们通过转录组数据筛选到意大利蜜蜂响应热激胁迫的热激蛋白家族的一个基因DnaJC28。本文旨在运用生物信息学的方法分析意大利蜜蜂DnaJC28理化性质、跨膜区、保守结构域、核定位和亚细胞定位、信号肽序列、修饰位点(磷酸化和糖基化)、同源性分析、亲缘关系、互作蛋白和蛋白质结构。理化性质分析得到:DnaJC28相对分子量约42389.89Da,含有115个氨基酸残基,是一种带正电的亲水性蛋白质。跨膜区预测分析结果显示:DnaJC28蛋白质不含有跨膜结构域,可能属于胞外蛋白。保守结构域预测显示:意大利蜜蜂DnaJC28蛋白质存在保守的J结构域,主要通过刺激重要伴侣Hsp70的ATP酶活性发挥作用。核定位和亚细胞定位预测结果显示:DnaJC28被预测为有极大的概率在细胞核中发挥作用,但发现在预测的DnaJC28编码蛋白中不存在经典的核定位信号。对此可解释为在热激胁迫条件下,定位于细胞质的亚型可以转移至细胞核内。信号肽预测结果显示:DnaJC28蛋白质无信号肽,属于非分泌性蛋白质。蛋白质修饰位点预测结果分析显示:DnaJC28蛋白质存在24个潜在的磷酸化位点和7个O-糖基化位点。蛋白质同源性预测结果显示:DnaJC28蛋白质具有保守性,可能在不同物种中发挥重要作用。亲缘关系预测结果显示:意大利蜜蜂的DnaJC28与蜜蜂属的大蜜蜂和蜜蜂科熊蜂属的欧洲熊蜂亲缘关系相近。蛋白质互作预测结果显示:意大利蜜蜂DnaJC28与Ac3和LOC552769这两种蛋白互作的可能性最高。蛋白质结构预测结果显示:二级结构主要包括α螺旋17个和无规则卷曲18个,不含β折叠结构。本研究可为进一步研究意大利蜜蜂DnaJC28的结构和功能提供参考。

The DnaJ gene family plays an important role in the response to heat stress in both animals and plants.In this study,we identified a gene called DnaJC28 in Apis mellifera that responds to heat stress based on transcriptome data analysis.The aim of this study was to analyze the physicochemical properties,transmembraneregions,conserved domains,nuclear localization,subcellular localization,signal peptide sequence,modification sites(phosphorylation and glycosylation),homology analysis,protein-protein interactions,and protein structure of DnaJC28 in Apis mellifera using bioinformatics methods.The phyaicochemical analyaia revcaled that DnaJC28 ha3 a relative molecular weight of approximately 42,389.89 Da and contains 115 amino acid residues.It is a positively charged hydrophilic protein.The analysis of transmembrane regions predicted that DnaJC28does not contain any transmembrane domains and is likely an extracellular protein.The prediction of conserved domains showed that DnaJC28 in Apis mellifera has a conserved J domain,which primarily functions by stimulating the ATPase activity of the important partner protein Hsp70.The prediction of nuclear localization and subcellular localization showed that DnaJC28 is highly likely to function in the cell nucleus but lacks a classical nuclear localization signal in the predicted protein sequence.This could be explained by the possibility that under heat stress conditions,the cytoplasmic subtype of DnaJC28 can be translocated into the nucleus.The prediction of signal peptides showed that DnaJC28 does not have a signal peptide and is a non-secretory protein.Analysis of protein modification sites showed that 24 potential phosphorylation sites and 7 O-glycosylation sites in DnaJC28.The prediction of protein homology revealed that DnaJC28 is conserved and likely plays an important role in different species.The prediction of phylogenetic relationships showed that DnaJC28 in Apis mellifera is closely related to the DnaJC28 of honey bees in the Apis genus and European honey bees in the Bombusgenus.TThepredictionof protein-protein interactions indicated that DnaJC28 in Apis mellifera is most likely to interact with Ac3 and LOC552769 proteins.The prediction of protein structure showed that the secondary structure of DnaJC28 primarily consists of 17α-helices and 18 random coils,without any β-folded structures.This study provides a reference for further research on the structure and function of DnaJC28 in Apis mellifera.