{"title":"Palmitoylation of the fission yeast protein Isp3 is essential for the formation of the outermost layer of the spore wall.","authors":"Takafumi Sakai, Nagisa Minomo, Tomoki Sakaguchi, Yuhei O Tahara, Makoto Miyata, Taro Nakamura","doi":"10.1093/bbb/zbaf104","DOIUrl":null,"url":null,"abstract":"<p><p>Fission yeast spores possess strong resistance to environmental stresses, largely due to the outermost proteinaceous \"Isp3 layer,\" which comprises Isp3 protein. Isp3 is palmitoylated, and its localization to the spore periphery is impaired in mutants lacking palmitoyltransferase; however, the precise role of Isp3 palmitoylation remains unclear. Here, we found that Isp3-GFP was expressed at wild-type levels in forming spores in mug142∆ cells lacking the palmitoyltransferase catalytic unit; thus, lack of palmitoylation did not reduce Isp3 protein stability. Next, we identified cysteine 7 as the key palmitoylation site essential for Isp3 localization to the spore periphery. Electron microscopy revealed that the Isp3 fibrillar layer was absent in both mug142Δ and isp3-C7S spores. Additionally, the isp3-C7S spores displayed increased sensitivity to alcohol stress, similar to isp3∆ spores. Collectively, these results demonstrate that palmitoylation of Isp3 is essential for the relocation of Isp3 to the spore surface and the assembly of the Isp3 layer.</p>","PeriodicalId":9175,"journal":{"name":"Bioscience, Biotechnology, and Biochemistry","volume":" ","pages":"1444-1455"},"PeriodicalIF":1.3000,"publicationDate":"2025-09-23","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Bioscience, Biotechnology, and Biochemistry","FirstCategoryId":"5","ListUrlMain":"https://doi.org/10.1093/bbb/zbaf104","RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q4","JCRName":"BIOCHEMISTRY & MOLECULAR BIOLOGY","Score":null,"Total":0}
引用次数: 0
Abstract
Fission yeast spores possess strong resistance to environmental stresses, largely due to the outermost proteinaceous "Isp3 layer," which comprises Isp3 protein. Isp3 is palmitoylated, and its localization to the spore periphery is impaired in mutants lacking palmitoyltransferase; however, the precise role of Isp3 palmitoylation remains unclear. Here, we found that Isp3-GFP was expressed at wild-type levels in forming spores in mug142∆ cells lacking the palmitoyltransferase catalytic unit; thus, lack of palmitoylation did not reduce Isp3 protein stability. Next, we identified cysteine 7 as the key palmitoylation site essential for Isp3 localization to the spore periphery. Electron microscopy revealed that the Isp3 fibrillar layer was absent in both mug142Δ and isp3-C7S spores. Additionally, the isp3-C7S spores displayed increased sensitivity to alcohol stress, similar to isp3∆ spores. Collectively, these results demonstrate that palmitoylation of Isp3 is essential for the relocation of Isp3 to the spore surface and the assembly of the Isp3 layer.
期刊介绍:
Bioscience, Biotechnology, and Biochemistry publishes high-quality papers providing chemical and biological analyses of vital phenomena exhibited by animals, plants, and microorganisms, the chemical structures and functions of their products, and related matters. The Journal plays a major role in communicating to a global audience outstanding basic and applied research in all fields subsumed by the Japan Society for Bioscience, Biotechnology, and Agrochemistry (JSBBA).