Roles of the HSP70-Subunit in a Eukaryotic Multi-Site-Specific Endonuclease, Endo. SceI : Autophosphorylation and Heat Stability
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概要
- 論文の詳細を見る
The 70 kDa heat shock proteins (HSP70) are a family of molecular chaperones that bind transiently to unfolded proteins in an ATP/ADP dependent manner. Endo.SceI comprises a unique example for mitochondrial HSP70, which exists in a stable complex with a nucleolytic subunit as a multi-site specific DNase. The HSP70-subunit in Endo.SceI was autophosphorylated by ATP in vitro. The autophosphorylation was higher in the Endo.SceI complex form than in the free form. Although the autophosphorylation had no significant effect on the endonucleolytic activity of Endo.SceI, the factors favoring autophosphorylation protected the endonucleolytic activity of Endo.SceI against heat inactivation. ATP, adenosine 5′-O-(3-thiotriphosphate) (ATP-γ-S), and ADP not only protected the endonucleolytic activity against heat inactivation in the presence of Ca2+ ions, but also reduced the labeling of the HSP70-subunit by [γ-32P]ATP in Endo.SceI. These findings suggest that the HSP70-subunit shields Endo.SceI from heat inactivation through ATP/ADP binding.
- 社団法人 日本農芸化学会の論文
- 2004-12-23
著者
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ITO Fumiaki
Department of Information Network Engineering, Musashi Institute of Technology
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Shibata Takehiko
Cellular and Molecular Biology Laboratory
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Ito Fumiaki
Department Of Biochemistry Faculty Of Pharmaceutical Sciences Setsunan University
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KAWASAKI Katsumi
Department of Biochemistry, Faculty of Pharmaceutical Sciences, Setsunan University
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SHIBATA Takehiko
Laboratory of Cellular and Molecular Biology, RIKEN (The Institute of Physical and Chemical Research
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Shibata Takehiko
Laboratory Of Cellular & Molecular Biology The Institute Of Physical And Chemical Research (rike
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Kawasaki Katsumi
Cellular And Molecular Biology Laboratory:department Of Biochemistry Faculty Of Pharmaceutical Scien
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