Variations in Heat Shock Proteins between Different Honey Bees and Bee Taxa Utilizing Bioinformatics

Hossam F. Abou-Shaara
{"title":"Variations in Heat Shock Proteins between Different Honey Bees and Bee Taxa Utilizing Bioinformatics","authors":"Hossam F. Abou-Shaara","doi":"10.31467/uluaricilik.1390515","DOIUrl":null,"url":null,"abstract":"The changes in climate and exposure of pollinators to heat stress are among the major concerns in the agricultural communities. Bees from different taxa have a great role in plant pollination. The exposure of bees to heat stress induces the expression of heat shock proteins (HSPs) to protect the body cells. Many studies have investigated the variations in the expression levels of HSPs and analyzed their amino acid sequences. Currently, databases for sequences of HSPs with different molecular weights are available. Variations in the expression levels of HSPs among individuals belong to the same bee taxa or different taxa exposed to heat stress have been noted. It is hypothesized that the properties of HSPs could help in understanding such variations. In this study, bioinformatics and other protein analysis tools were utilized to shade lights on the variations between sequences of heat shock proteins 60 (HSP60) and 83 (HSP83) in 18 bee taxa (15 from Family Apidae, 2 from Family Halictidae, and one from Megachilidae). The analysis of amino acids and nucleotides showed some identical values to bees from genus Apis and Bombus. The conserved domains were highly identical in case of HSP60 than HSP83. The motifs were from one or more protein families with variation among taxa. All proteins showed hydrophilic properties with variable isoelectric points. The study suggested an identical 3-D structure for proteins in all bee taxa. The role of the detected variations in affecting the response of HSPs to stress was discussed. This study paves the way for more investigations on HSPs and encourages the use of bioinformatics and protein analysis tools to explain any observable variations.","PeriodicalId":104346,"journal":{"name":"Uludağ Arıcılık Dergisi","volume":"78 5-6","pages":""},"PeriodicalIF":0.0000,"publicationDate":"2024-02-07","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Uludağ Arıcılık Dergisi","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.31467/uluaricilik.1390515","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 0

Abstract

The changes in climate and exposure of pollinators to heat stress are among the major concerns in the agricultural communities. Bees from different taxa have a great role in plant pollination. The exposure of bees to heat stress induces the expression of heat shock proteins (HSPs) to protect the body cells. Many studies have investigated the variations in the expression levels of HSPs and analyzed their amino acid sequences. Currently, databases for sequences of HSPs with different molecular weights are available. Variations in the expression levels of HSPs among individuals belong to the same bee taxa or different taxa exposed to heat stress have been noted. It is hypothesized that the properties of HSPs could help in understanding such variations. In this study, bioinformatics and other protein analysis tools were utilized to shade lights on the variations between sequences of heat shock proteins 60 (HSP60) and 83 (HSP83) in 18 bee taxa (15 from Family Apidae, 2 from Family Halictidae, and one from Megachilidae). The analysis of amino acids and nucleotides showed some identical values to bees from genus Apis and Bombus. The conserved domains were highly identical in case of HSP60 than HSP83. The motifs were from one or more protein families with variation among taxa. All proteins showed hydrophilic properties with variable isoelectric points. The study suggested an identical 3-D structure for proteins in all bee taxa. The role of the detected variations in affecting the response of HSPs to stress was discussed. This study paves the way for more investigations on HSPs and encourages the use of bioinformatics and protein analysis tools to explain any observable variations.
利用生物信息学研究不同蜜蜂和蜜蜂类群之间热休克蛋白的差异
气候的变化和传粉昆虫面临的热胁迫是农业界关注的主要问题之一。不同类群的蜜蜂在植物授粉中发挥着重要作用。蜜蜂暴露在热应激中会诱导热休克蛋白(HSPs)的表达,以保护体细胞。许多研究调查了热休克蛋白表达水平的变化,并分析了其氨基酸序列。目前,已有不同分子量的 HSP 序列数据库。人们注意到,属于同一蜜蜂类群或不同类群的蜜蜂暴露于热应激时,其 HSPs 的表达水平存在差异。据推测,HSPs 的特性有助于理解这种变化。本研究利用生物信息学和其他蛋白质分析工具,研究了 18 个蜜蜂类群(15 个蜜蜂类群来自喙蜂科,2 个蜜蜂类群来自卤虫科,1 个蜜蜂类群来自姬蜂科)的热休克蛋白 60(HSP60)和 83(HSP83)序列之间的差异。对氨基酸和核苷酸的分析表明,有些值与蜂属和蜂属蜜蜂相同。与 HSP83 相比,HSP60 的保守结构域高度一致。在不同类群中,这些基序来自一个或多个蛋白家族。所有蛋白质都具有亲水性,等电点各不相同。研究表明,所有蜜蜂类群的蛋白质都具有相同的三维结构。研究还讨论了检测到的变异在影响 HSPs 对应激反应中的作用。这项研究为更多关于HSP的研究铺平了道路,并鼓励使用生物信息学和蛋白质分析工具来解释任何可观察到的变异。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
求助全文
约1分钟内获得全文 求助全文
来源期刊
自引率
0.00%
发文量
0
×
引用
GB/T 7714-2015
复制
MLA
复制
APA
复制
导出至
BibTeX EndNote RefMan NoteFirst NoteExpress
×
提示
您的信息不完整,为了账户安全,请先补充。
现在去补充
×
提示
您因"违规操作"
具体请查看互助需知
我知道了
×
提示
确定
请完成安全验证×
copy
已复制链接
快去分享给好友吧!
我知道了
右上角分享
点击右上角分享
0
联系我们:info@booksci.cn Book学术提供免费学术资源搜索服务,方便国内外学者检索中英文文献。致力于提供最便捷和优质的服务体验。 Copyright © 2023 布克学术 All rights reserved.
京ICP备2023020795号-1
ghs 京公网安备 11010802042870号
Book学术文献互助
Book学术文献互助群
群 号:481959085
Book学术官方微信