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庆大霉素通过干扰底物识别来抑制 HSP70 辅助的蛋白质折叠。

Gentamicin inhibits HSP70-assisted protein folding by interfering with substrate recognition.

机构信息

Department of Life Science, Faculty of Engineering and Resource Science, Akita University, Akita City, Japan.

出版信息

FEBS Lett. 2010 Feb 19;584(4):645-51. doi: 10.1016/j.febslet.2009.12.021. Epub 2009 Dec 22.

Abstract

We previously reported that gentamicin (GM) specifically binds to heat-shock protein with subunit molecular masses of 70 kDa (HSP70). In the present study, we have investigated the effects of GM binding on HSP70-assisted protein folding in vitro. The C-terminal, and not the N-terminal of HSP70 was found to bind to GM. GM significantly suppressed refolding of firefly luciferase in the presence of HSP70 and HSP40, although the ATPase activity of HSP70 was unaffected by GM. A surface plasmon resonance analysis revealed that GM specifically interferes with the binding of HSP70 to a model peptide that mimics the exposed hydrophobic surface of the folding intermediates. These results indicated that GM inhibits the chaperone activity of HSP70 and may suppress protein folding via inhibition of HSP70 in vivo.

摘要

我们之前曾报道庆大霉素(GM)能特异性地与分子量为 70 kDa 的热休克蛋白(HSP70)结合。在本研究中,我们研究了 GM 结合对 HSP70 辅助的体外蛋白质折叠的影响。发现 HSP70 的 C 端而不是 N 端与 GM 结合。尽管 GM 对 HSP70 的 ATP 酶活性没有影响,但 GM 显著抑制了在 HSP70 和 HSP40 存在下萤火虫荧光素的重折叠。表面等离子体共振分析表明 GM 特异性地干扰 HSP70 与模拟折叠中间体暴露的疏水面的模型肽的结合。这些结果表明 GM 抑制 HSP70 的伴侣活性,并可能通过抑制 HSP70 在体内抑制蛋白质折叠。

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