{"title":"木贼热休克蛋白基因超家族的全基因组鉴定和表达分析","authors":"Xiaozhuo Zong, Yabei Xu, Jing Tao","doi":"10.1016/j.cbd.2024.101284","DOIUrl":null,"url":null,"abstract":"<div><p><em>Hylurgus ligniperda</em> belongs to <em>Hylurgus Latreille</em>, Curculionidae, Coleoptera. It primarily damages the base and roots of the trunk of pine plants. Short-term treatment at 42 °C can damage <em>Hylurgus ligniperda</em>; therefore, temperature is a vital factor limiting its spread. Heat shock proteins (HSPs) can protect, remove, and repair proteins to help <em>H. ligniperda</em> withstand high temperatures. However, information on HSP genes in <em>H. ligniperda</em> remains limited. In the study, we considered <em>H. ligniperda</em> as the focus of research and identified 56 <em>HligHSP</em> genes at the genome-wide level. These genes were mapped to the cytoplasm or nucleus. An identical subfamily exhibited a closely similar distribution of conserved domains. Combined with the transcriptome data collected in previous studies, we screened six candidate genes, namely <em>HligsHSP-3</em>, <em>HligsHSP-4</em>, <em>HligHSP60-16</em>, <em>HligHSP70-3</em>, <em>HligHSP70-4</em>, and <em>HligHSP90-1</em>, which are specifically expressed during different high-temperature treatments. A quantitative polymerase chain reaction was performed to measure the expression of these six <em>HligHSPs</em> in seven temperature treatment conditions. These genes may be involved in the heat resistance mechanism in adults. Our findings provided a foundation for further studying the heat resistance mechanism in <em>H. ligniperda</em>.</p></div>","PeriodicalId":2,"journal":{"name":"ACS Applied Bio Materials","volume":null,"pages":null},"PeriodicalIF":4.6000,"publicationDate":"2024-07-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"Genome-wide identification and expression analysis of the heat shock protein gene superfamily in Hylurgus ligniperda\",\"authors\":\"Xiaozhuo Zong, Yabei Xu, Jing Tao\",\"doi\":\"10.1016/j.cbd.2024.101284\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<div><p><em>Hylurgus ligniperda</em> belongs to <em>Hylurgus Latreille</em>, Curculionidae, Coleoptera. It primarily damages the base and roots of the trunk of pine plants. Short-term treatment at 42 °C can damage <em>Hylurgus ligniperda</em>; therefore, temperature is a vital factor limiting its spread. Heat shock proteins (HSPs) can protect, remove, and repair proteins to help <em>H. ligniperda</em> withstand high temperatures. However, information on HSP genes in <em>H. ligniperda</em> remains limited. In the study, we considered <em>H. ligniperda</em> as the focus of research and identified 56 <em>HligHSP</em> genes at the genome-wide level. These genes were mapped to the cytoplasm or nucleus. An identical subfamily exhibited a closely similar distribution of conserved domains. Combined with the transcriptome data collected in previous studies, we screened six candidate genes, namely <em>HligsHSP-3</em>, <em>HligsHSP-4</em>, <em>HligHSP60-16</em>, <em>HligHSP70-3</em>, <em>HligHSP70-4</em>, and <em>HligHSP90-1</em>, which are specifically expressed during different high-temperature treatments. A quantitative polymerase chain reaction was performed to measure the expression of these six <em>HligHSPs</em> in seven temperature treatment conditions. These genes may be involved in the heat resistance mechanism in adults. Our findings provided a foundation for further studying the heat resistance mechanism in <em>H. ligniperda</em>.</p></div>\",\"PeriodicalId\":2,\"journal\":{\"name\":\"ACS Applied Bio Materials\",\"volume\":null,\"pages\":null},\"PeriodicalIF\":4.6000,\"publicationDate\":\"2024-07-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"ACS Applied Bio Materials\",\"FirstCategoryId\":\"99\",\"ListUrlMain\":\"https://www.sciencedirect.com/science/article/pii/S1744117X24000972\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q2\",\"JCRName\":\"MATERIALS SCIENCE, BIOMATERIALS\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"ACS Applied Bio Materials","FirstCategoryId":"99","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/S1744117X24000972","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q2","JCRName":"MATERIALS SCIENCE, BIOMATERIALS","Score":null,"Total":0}
Genome-wide identification and expression analysis of the heat shock protein gene superfamily in Hylurgus ligniperda
Hylurgus ligniperda belongs to Hylurgus Latreille, Curculionidae, Coleoptera. It primarily damages the base and roots of the trunk of pine plants. Short-term treatment at 42 °C can damage Hylurgus ligniperda; therefore, temperature is a vital factor limiting its spread. Heat shock proteins (HSPs) can protect, remove, and repair proteins to help H. ligniperda withstand high temperatures. However, information on HSP genes in H. ligniperda remains limited. In the study, we considered H. ligniperda as the focus of research and identified 56 HligHSP genes at the genome-wide level. These genes were mapped to the cytoplasm or nucleus. An identical subfamily exhibited a closely similar distribution of conserved domains. Combined with the transcriptome data collected in previous studies, we screened six candidate genes, namely HligsHSP-3, HligsHSP-4, HligHSP60-16, HligHSP70-3, HligHSP70-4, and HligHSP90-1, which are specifically expressed during different high-temperature treatments. A quantitative polymerase chain reaction was performed to measure the expression of these six HligHSPs in seven temperature treatment conditions. These genes may be involved in the heat resistance mechanism in adults. Our findings provided a foundation for further studying the heat resistance mechanism in H. ligniperda.