Oligomerization properties of Rat Heat Shock Protein 86
碩士 === 國立清華大學 === 分子與細胞生物研究所 === 92 === Heat shock protein 90 (HSP90) is an abundant chaperone in the cytosol, including two isoforms α and β. The rat homologue of HSP90 was HSP86, and defined as four domains in this study: N-terminal domain (a.a. 1~237), highly charged linker domain (a.a. 238~272)...
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ndltd-TW-092NTHU50610142015-10-13T13:08:02Z http://ndltd.ncl.edu.tw/handle/51134327332785564665 Oligomerization properties of Rat Heat Shock Protein 86 老鼠熱休克蛋白八十六之多聚體特性研究 Ya-Lun Shen 沈雅倫 碩士 國立清華大學 分子與細胞生物研究所 92 Heat shock protein 90 (HSP90) is an abundant chaperone in the cytosol, including two isoforms α and β. The rat homologue of HSP90 was HSP86, and defined as four domains in this study: N-terminal domain (a.a. 1~237), highly charged linker domain (a.a. 238~272), middle domain (a.a. 273~538) and C-terminal domain (a.a. 539~733). The chaperone activity of HSP90 is modulated by ATP hydrolysis and by interacting with several co-chaperones. In addition, heat-induced transition of HSP90 to self-oligomerization was also necessary for exerting the chaperone activity. Here, we used three HSP86 recombinants (HSP86N a.a. 1~237, HSP86NM a.a 1~538, HSP86C a.a 539~733) to explore the properties of oligomerization in each domain. From suppression assay, oligomerization of HSP86-N and HSP86-C resulted in higher chaperone function, whereas that of HSP86-NM showed lower chaperone function. We assumed that the oligomerization region in the middle domain overlapped with client binding domain. The N-terminal domain has lower critical temperature than the C-terminal domain, suggesting the first step of oligomerization of full length HSP86 starts from N-terminal. The oligomerization of HSP86-N and HSP86-C was affected by factors including ATP, ADP, Ca+ and Zn+, indicating there may be binding site for each factor. Margaret Dah-Tsyr Chang 張大慈 2004 學位論文 ; thesis 74 en_US |
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碩士 === 國立清華大學 === 分子與細胞生物研究所 === 92 === Heat shock protein 90 (HSP90) is an abundant chaperone in the cytosol, including two isoforms α and β. The rat homologue of HSP90 was HSP86, and defined as four domains in this study: N-terminal domain (a.a. 1~237), highly charged linker domain (a.a. 238~272), middle domain (a.a. 273~538) and C-terminal domain (a.a. 539~733). The chaperone activity of HSP90 is modulated by ATP hydrolysis and by interacting with several co-chaperones. In addition, heat-induced transition of HSP90 to self-oligomerization was also necessary for exerting the chaperone activity. Here, we used three HSP86 recombinants (HSP86N a.a. 1~237, HSP86NM a.a 1~538, HSP86C a.a 539~733) to explore the properties of oligomerization in each domain. From suppression assay, oligomerization of HSP86-N and HSP86-C resulted in higher chaperone function, whereas that of HSP86-NM showed lower chaperone function. We assumed that the oligomerization region in the middle domain overlapped with client binding domain. The N-terminal domain has lower critical temperature than the C-terminal domain, suggesting the first step of oligomerization of full length HSP86 starts from N-terminal. The oligomerization of HSP86-N and HSP86-C was affected by factors including ATP, ADP, Ca+ and Zn+, indicating there may be binding site for each factor.
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Margaret Dah-Tsyr Chang |
author_facet |
Margaret Dah-Tsyr Chang Ya-Lun Shen 沈雅倫 |
author |
Ya-Lun Shen 沈雅倫 |
spellingShingle |
Ya-Lun Shen 沈雅倫 Oligomerization properties of Rat Heat Shock Protein 86 |
author_sort |
Ya-Lun Shen |
title |
Oligomerization properties of Rat Heat Shock Protein 86 |
title_short |
Oligomerization properties of Rat Heat Shock Protein 86 |
title_full |
Oligomerization properties of Rat Heat Shock Protein 86 |
title_fullStr |
Oligomerization properties of Rat Heat Shock Protein 86 |
title_full_unstemmed |
Oligomerization properties of Rat Heat Shock Protein 86 |
title_sort |
oligomerization properties of rat heat shock protein 86 |
publishDate |
2004 |
url |
http://ndltd.ncl.edu.tw/handle/51134327332785564665 |
work_keys_str_mv |
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