Palmitoylation of the fission yeast protein Isp3 is essential for the formation of the outermost layer of the spore wall.

IF 1.3 4区 生物学 Q4 BIOCHEMISTRY & MOLECULAR BIOLOGY
Takafumi Sakai, Nagisa Minomo, Tomoki Sakaguchi, Yuhei O Tahara, Makoto Miyata, Taro Nakamura
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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.

裂变酵母蛋白Isp3的棕榈酰化对孢子壁最外层的形成至关重要。
裂变酵母孢子具有很强的抗环境胁迫能力,这主要是由于最外层含有Isp3蛋白的“Isp3层”。在缺乏棕榈酰转移酶的突变体中,Isp3被棕榈酰化,其在孢子周围的定位受损;然而,Isp3棕榈酰化的确切作用尚不清楚。在这里,我们发现Isp3-GFP在缺乏棕榈酰转移酶催化单元的mug142∆细胞中以野生型水平表达形成孢子;因此,缺乏棕榈酰化并不会降低Isp3蛋白的稳定性。接下来,我们确定了半胱氨酸7是Isp3定位到孢子周围所必需的关键棕榈酰化位点。电镜显示mug142Δ和Isp3 - c7s孢子中均无Isp3纤维层。此外,isp3- c7s孢子对酒精胁迫的敏感性增加,与isp3∆孢子相似。总的来说,这些结果表明Isp3的棕榈酰化对于Isp3重新定位到孢子表面和Isp3层的组装是必不可少的。
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来源期刊
Bioscience, Biotechnology, and Biochemistry
Bioscience, Biotechnology, and Biochemistry 生物-生化与分子生物学
CiteScore
3.50
自引率
0.00%
发文量
183
审稿时长
1 months
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).
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