Asp73とAsp420は酵母ミトコンドリアHsp60のATP加水分解に重要な役割を果たす --材料分析室利用研究成果、そのXXXI(1)
| Autor: | Masuda, Megumi, Murakoshi, Nodoka, Yoda, Hiromi, Koike-Takeshita, Ayumi |
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| Jazyk: | japonština |
| Rok vydání: | 2021 |
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| Zdroj: | 神奈川工科大学研究報告.B,理工学編. 45:27-33 |
| ISSN: | 2188-2878 |
| Popis: | application/pdf Type I chaperonins (Cpn60/Hsp60) are essential proteins that mediate the correct folding of newly translated and stress-denatured proteins in bacteria, chloroplast and mitochondria. Despite the high sequence homology among chaperonins, there are some critical differences at the mechanistic level between the bacterial and the mitochondrial chaperonins with respect to their oligomeric state and their ability to function with co-chaperonins from different sources. Asp52 and Asp398 in Escherichia coli chaperonin GroEL are known as the critical residues on ATP hydrolysis because GroELD52A/D398A mutant is severely deficient in ATP hydrolysis but not in ATP binding. Here, yeast mitochondria Hsp60 (mHsp60) and Thermus thermophilus Hsp60 (TCpn60) were used to investigate the functional commonality of these two well-conserved Asp in ATP hydrolysis. These residues in GroEL correspond to Asp73 and Asp420 in mHsp60 and to Asp51 and Asp396 in TCpn60, respectively. We found that ATPase activity of mHsp60D73A and mHsp60D420A mutants were ~20% and < 4% of wild type, respectively, indicating that functional commonality of two Asp was shown in yeast mHsp60, despite suggesting different roles of Asp51 in TCpn60, surprisingly. |
| Databáze: | OpenAIRE |
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