Takasaki Teruaki, Tomimoto Naofumi, Ikehata Takumi, Satoh Ryosuke, Sugiura Reiko
Laboratory of Molecular Pharmacogenomics, Department of Pharmaceutical Sciences, Faculty of Pharmacy, Kindai University.
MicroPubl Biol. 2021 May 4;2021. doi: 10.17912/micropub.biology.000388.
The molecular chaperone Hsp90 is highly conserved from bacteria to mammals. In fission yeast, Hsp90 is essential in many cellular processes and its expression is known to be increased by heat stress (HS). Here, we describe the distinct spatiotemporal distribution of Hsp90 under high-heat stress (HHS: 45˚C) and mild-heat stress (MHS: 37˚C). Hsp90 is largely distributed in the cytoplasm under non-stressed conditions (27˚C). Under HHS, Hsp90 forms several cytoplasmic granules within 5 minutes, then the granules disappear within 60 minutes. Under MHS, Hsp90 forms fewer granules than under HHS within 5 minutes and strikingly the granules persist and grow in size. In addition, nuclear enrichment of Hsp90 was observed after 60 minutes under both HS conditions. Our data suggest that assembly/disassembly of Hsp90 granules is differentially regulated by temperatures.
分子伴侣Hsp90从细菌到哺乳动物都高度保守。在裂殖酵母中，Hsp90在许多细胞过程中至关重要，并且已知其表达会因热应激（HS）而增加。在此，我们描述了在高热应激（HHS：45˚C）和低热应激（MHS：37˚C）下Hsp90独特的时空分布。在非应激条件（27˚C）下，Hsp90主要分布在细胞质中。在HHS下，Hsp90在5分钟内形成几个细胞质颗粒，然后这些颗粒在60分钟内消失。在MHS下，Hsp90在5分钟内形成的颗粒比在HHS下少，并且显著的是，这些颗粒持续存在并增大尺寸。此外，在两种热应激条件下60分钟后均观察到Hsp90在细胞核中的富集。我们的数据表明，Hsp90颗粒的组装/拆卸受温度的差异调节。
