Robert A. Aspbury, Mark C. Prescott, Michael J. Fisher, Huw H. Rees
{"title":"秀丽隐杆线虫多肽的异戊二烯化","authors":"Robert A. Aspbury, Mark C. Prescott, Michael J. Fisher, Huw H. Rees","doi":"10.1016/S0005-2760(98)00040-X","DOIUrl":null,"url":null,"abstract":"<div><p>Covalent modification of eucaryotic proteins, involving addition of isoprenyl groups, is a widespread phenomenon. Here we provide direct evidence for this form of covalent modification in the free-living nematode, <em>Caenorhabditis elegans</em>. Following incubation in the presence of [<sup>3</sup>H]mevalonolactone, specific <em>C. elegans</em> polypeptides became labelled in both aqueous and detergent (Triton X-114)-enriched extracts. Chemical and GC–MS analysis of modifying groups, cleaved from <em>C. elegans</em> polypeptides, revealed that geranylgeranylation and, to a lesser extent, farnesylation of target polypeptides occurred. Immunoblot analysis provided preliminary evidence that the <em>ras</em>-like <em>let-60</em> polypeptide was a target for isoprenylation in <em>C. elegans</em>.</p></div>","PeriodicalId":100162,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism","volume":"1392 2","pages":"Pages 265-275"},"PeriodicalIF":0.0000,"publicationDate":"1998-06-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0005-2760(98)00040-X","citationCount":"6","resultStr":"{\"title\":\"Isoprenylation of polypeptides in the nematode Caenorhabditis elegans\",\"authors\":\"Robert A. Aspbury, Mark C. Prescott, Michael J. Fisher, Huw H. Rees\",\"doi\":\"10.1016/S0005-2760(98)00040-X\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<div><p>Covalent modification of eucaryotic proteins, involving addition of isoprenyl groups, is a widespread phenomenon. Here we provide direct evidence for this form of covalent modification in the free-living nematode, <em>Caenorhabditis elegans</em>. Following incubation in the presence of [<sup>3</sup>H]mevalonolactone, specific <em>C. elegans</em> polypeptides became labelled in both aqueous and detergent (Triton X-114)-enriched extracts. Chemical and GC–MS analysis of modifying groups, cleaved from <em>C. elegans</em> polypeptides, revealed that geranylgeranylation and, to a lesser extent, farnesylation of target polypeptides occurred. Immunoblot analysis provided preliminary evidence that the <em>ras</em>-like <em>let-60</em> polypeptide was a target for isoprenylation in <em>C. elegans</em>.</p></div>\",\"PeriodicalId\":100162,\"journal\":{\"name\":\"Biochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism\",\"volume\":\"1392 2\",\"pages\":\"Pages 265-275\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"1998-06-15\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://sci-hub-pdf.com/10.1016/S0005-2760(98)00040-X\",\"citationCount\":\"6\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Biochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://www.sciencedirect.com/science/article/pii/S000527609800040X\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Biochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism","FirstCategoryId":"1085","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/S000527609800040X","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
Isoprenylation of polypeptides in the nematode Caenorhabditis elegans
Covalent modification of eucaryotic proteins, involving addition of isoprenyl groups, is a widespread phenomenon. Here we provide direct evidence for this form of covalent modification in the free-living nematode, Caenorhabditis elegans. Following incubation in the presence of [3H]mevalonolactone, specific C. elegans polypeptides became labelled in both aqueous and detergent (Triton X-114)-enriched extracts. Chemical and GC–MS analysis of modifying groups, cleaved from C. elegans polypeptides, revealed that geranylgeranylation and, to a lesser extent, farnesylation of target polypeptides occurred. Immunoblot analysis provided preliminary evidence that the ras-like let-60 polypeptide was a target for isoprenylation in C. elegans.