Glycine at the 65th position plays an essential role in ATP-dependent protein folding by Archael group II chaperonin.
Glycine at the 65th position plays an essential role in ATP-dependent protein folding by Archael group II chaperonin.
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第 65 位的甘氨酸在 Archael II 族伴侣蛋白的 ATP 依赖性蛋白质折叠中起着重要作用。
DOI：
10.1006/bbrc.2001.6139
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发表时间：
2001
影响因子：
3.1
通讯作者：
M. Yohda
中科院分区：
文献类型：
--
作者：
R. Iizuka;T. Yoshida;T. Maruyama;Y. Shomura;K. Miki;M. Yohda
在先前的研究中，我们已经发现，G65 C和I125 T双突变体的α伴侣蛋白同源寡聚体从超嗜热古菌，Thermococcus sp.菌株KS-1，缺乏ATP依赖的蛋白质重折叠活性，尽管显示ATP酶活性和结合变性蛋白的能力。在这项研究中，我们已经确定了几个突变的热球菌伴侣蛋白同源寡聚体与Gly-65或Ile-125的氨基酸取代。结果表明，第65位氨基酸残基应该是一个小的氨基酸，如甘氨酸或丙氨酸的ATP依赖性复性活性。用侧链大于甲基的氨基酸取代Gly-65的α伴侣蛋白同源寡聚物不具有ATP依赖性蛋白质重折叠活性，但在ATP或AMP-PNP存在下表现出对未折叠蛋白质的结合亲和力增加。（c）2001年爱思唯尔科学。
In the previous study, we have found that G65C and I125T double mutant of alpha chaperonin homo-oligomer from a hyperthermophilic archaeum, Thermococcus sp. strain KS-1, lacks ATP-dependent protein refolding activity despite showing ATPase activity and the ability to bind the denatured proteins. In this study, we have characterized several mutant Thermococcus chaperonin homo-oligomers with the amino acid substitutions of Gly-65 or Ile-125. The results showed that amino acid residue at 65th position should be a small amino acid such as glycine or alanine for the ATP-dependent refolding activity. The alpha chaperonin homo-oligomers with amino acid substitution of Gly-65 by amino acids whose side chains are larger than the methyl group did not have ATP-dependent protein refolding activity, but exhibited an increase of the binding affinity for unfolded proteins in the presence of ATP or AMP-PNP. (c)2001 Elsevier Science.