Jinxuan Shi , Mingjun Fu , Chao Zhao , Falin Zhou , Qibin Yang , Lihua Qiu
{"title":"不同急性胁迫下黑虎虾 Hsp60 和 Hsp10 的特征和功能分析","authors":"Jinxuan Shi , Mingjun Fu , Chao Zhao , Falin Zhou , Qibin Yang , Lihua Qiu","doi":"10.1007/s12192-015-0660-6","DOIUrl":null,"url":null,"abstract":"<div><div>Heat shock proteins (Hsps) are a class of highly conserved proteins produced in virtually all living organisms from bacteria to humans. Hsp60 and Hsp10, the most important mitochondrial chaperones, participate in environmental stress responses. In this study, the full-length complementary DNAs (cDNAs) of Hsp60 (<em>PmHsp60</em>) and Hsp10 (<em>PmHsp10</em>) were cloned from <em>Penaeus monodon</em>. Sequence analysis showed that <em>PmHsp60</em> and <em>PmHsp10</em> encoded polypeptides of 578 and 102 amino acids, respectively. The expression profiles of <em>PmHsp60</em> and <em>PmHsp10</em> were detected in the gills and hepatopancreas of the shrimps under pH challenge, osmotic stress, and heavy metal exposure, and results suggested that <em>PmHsp60</em> and <em>PmHsp10</em> were involved in the responses to these stimuli. ATPase and chaperone activity assay indicated that <em>PmHsp60</em> could slow down protein denaturation and that Hsp60/Hsp10 may be combined to produce a chaperone complex with effective chaperone and ATPase activities. Overall, this study provides useful information to help further understand the functional mechanisms of the environmental stress responses of Hsp60 and Hsp10 in shrimp.</div></div>","PeriodicalId":9684,"journal":{"name":"Cell Stress & Chaperones","volume":"21 2","pages":"Pages 295-312"},"PeriodicalIF":3.3000,"publicationDate":"2016-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4786529/pdf/","citationCount":"0","resultStr":"{\"title\":\"Characterization and function analysis of Hsp60 and Hsp10 under different acute stresses in black tiger shrimp, Penaeus monodon\",\"authors\":\"Jinxuan Shi , Mingjun Fu , Chao Zhao , Falin Zhou , Qibin Yang , Lihua Qiu\",\"doi\":\"10.1007/s12192-015-0660-6\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<div><div>Heat shock proteins (Hsps) are a class of highly conserved proteins produced in virtually all living organisms from bacteria to humans. Hsp60 and Hsp10, the most important mitochondrial chaperones, participate in environmental stress responses. In this study, the full-length complementary DNAs (cDNAs) of Hsp60 (<em>PmHsp60</em>) and Hsp10 (<em>PmHsp10</em>) were cloned from <em>Penaeus monodon</em>. Sequence analysis showed that <em>PmHsp60</em> and <em>PmHsp10</em> encoded polypeptides of 578 and 102 amino acids, respectively. The expression profiles of <em>PmHsp60</em> and <em>PmHsp10</em> were detected in the gills and hepatopancreas of the shrimps under pH challenge, osmotic stress, and heavy metal exposure, and results suggested that <em>PmHsp60</em> and <em>PmHsp10</em> were involved in the responses to these stimuli. ATPase and chaperone activity assay indicated that <em>PmHsp60</em> could slow down protein denaturation and that Hsp60/Hsp10 may be combined to produce a chaperone complex with effective chaperone and ATPase activities. Overall, this study provides useful information to help further understand the functional mechanisms of the environmental stress responses of Hsp60 and Hsp10 in shrimp.</div></div>\",\"PeriodicalId\":9684,\"journal\":{\"name\":\"Cell Stress & Chaperones\",\"volume\":\"21 2\",\"pages\":\"Pages 295-312\"},\"PeriodicalIF\":3.3000,\"publicationDate\":\"2016-03-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4786529/pdf/\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Cell Stress & Chaperones\",\"FirstCategoryId\":\"99\",\"ListUrlMain\":\"https://www.sciencedirect.com/science/article/pii/S1355814523004340\",\"RegionNum\":3,\"RegionCategory\":\"生物学\",\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q3\",\"JCRName\":\"CELL BIOLOGY\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Cell Stress & Chaperones","FirstCategoryId":"99","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/S1355814523004340","RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q3","JCRName":"CELL BIOLOGY","Score":null,"Total":0}
Characterization and function analysis of Hsp60 and Hsp10 under different acute stresses in black tiger shrimp, Penaeus monodon
Heat shock proteins (Hsps) are a class of highly conserved proteins produced in virtually all living organisms from bacteria to humans. Hsp60 and Hsp10, the most important mitochondrial chaperones, participate in environmental stress responses. In this study, the full-length complementary DNAs (cDNAs) of Hsp60 (PmHsp60) and Hsp10 (PmHsp10) were cloned from Penaeus monodon. Sequence analysis showed that PmHsp60 and PmHsp10 encoded polypeptides of 578 and 102 amino acids, respectively. The expression profiles of PmHsp60 and PmHsp10 were detected in the gills and hepatopancreas of the shrimps under pH challenge, osmotic stress, and heavy metal exposure, and results suggested that PmHsp60 and PmHsp10 were involved in the responses to these stimuli. ATPase and chaperone activity assay indicated that PmHsp60 could slow down protein denaturation and that Hsp60/Hsp10 may be combined to produce a chaperone complex with effective chaperone and ATPase activities. Overall, this study provides useful information to help further understand the functional mechanisms of the environmental stress responses of Hsp60 and Hsp10 in shrimp.
期刊介绍:
Cell Stress and Chaperones is an integrative journal that bridges the gap between laboratory model systems and natural populations. The journal captures the eclectic spirit of the cellular stress response field in a single, concentrated source of current information. Major emphasis is placed on the effects of climate change on individual species in the natural environment and their capacity to adapt. This emphasis expands our focus on stress biology and medicine by linking climate change effects to research on cellular stress responses of animals, micro-organisms and plants.