PAN, the proteasome-activating nucleotidase from archaebacteria, is a protein-unfolding molecular chaperone
PAN, the proteasome-activating nucleotidase from archaebacteria, is a protein-unfolding molecular chaperone
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DOI：
10.1038/35041081
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发表时间：
2000-11-01
影响因子：
21.3
通讯作者：
Goldberg, AL
中科院分区：
文献类型：
--
作者：
Benaroudj, N;Goldberg, AL
詹氏甲烷球菌的蛋白酶体激活核苷酸酶（PAN）是一种相对分子质量为650，000的复合物，与真核生物26S蛋白酶体中的ATP酶同源。当与20S古细菌蛋白酶体和ATP混合时，PAN刺激蛋白质降解。在这里，我们表明，PAN减少变性蛋白质的聚集和增强其重折叠，这些过程不需要ATP水解，虽然ATP结合增强PAN的能力，以防止聚集。PAN还催化绿色荧光蛋白的解折叠，在其羧基末端具有11个残基的ssrA延伸（GFP 11）。这种解折叠需要ATP水解，并且当20S蛋白酶体也存在时与GFP 11降解有关。这种展开活动似乎是必不可少的ATP依赖的蛋白水解，虽然PAN本身可以作为一个分子伴侣。
The proteasome-activating nucleotidase (PAN) from Methanococcus jannaschii is a complex of relative molecular mass 650,000 that is homologous to the ATPases in the eukaryotic 26S proteasome. When mixed with 20S archaeal proteasomes and ATP, PAN stimulates protein degradation. Here we show that PAN reduces aggregation of denatured proteins and enhances their refolding, these processes do not require ATP hydrolysis, although ATP binding enhances the ability of PAN to prevent aggregation. PAN also catalyses the unfolding of the green fluorescent protein with an 11-residue ssrA extension at its carboxy terminus (GFP11). This unfolding requires ATP hydrolysis, and is linked to GFP11 degradation when 20S proteasomes are also present. This unfolding activity seems to be essential for ATP-dependent proteolysis, although PAN may function by itself as a molecular chaperone.