酵母热休克蛋白110（Sse1p）表现出高亲和力的肽结合特性。
The yeast Hsp110, Sse1p, exhibits high-affinity peptide binding.
作者信息
Goeckeler Jennifer L, Petruso Anthony P, Aguirre Julia, Clement Cristina C, Chiosis Gabriela, Brodsky Jeffrey L
机构信息
University of Pittsburgh, Department of Biological Sciences, 274A Crawford Hall, Pittsburgh, PA 15260, USA.
出版信息
FEBS Lett. 2008 Jul 9;582(16):2393-6. doi: 10.1016/j.febslet.2008.05.047. Epub 2008 Jun 6.
Abstract
Hsp110s are divergent relatives of Hsp70 chaperones that hydrolyze ATP. Hsp110s serve as Hsp70 nucleotide exchange factors and act directly to maintain polypeptide solubility. To date, the impact of peptide binding on Hsp110 ATPase activity is unknown and an Hsp110/peptide affinity has not been measured. We now report on a peptide that binds to the yeast Hsp110, Sse1p, with a K(D) of approximately 2 nM. Surprisingly, the binding of this peptide fails to stimulate Sse1p ATP hydrolysis. Moreover, an Hsp70-binding peptide is unable to associate with Sse1p, suggesting that Hsp70s and Hsp110s possess partially distinct peptide recognition motifs.
摘要
Hsp110是水解ATP的Hsp70伴侣蛋白的不同亲属。Hsp110作为Hsp70核苷酸交换因子，直接作用于维持多肽的溶解性。迄今为止，肽结合对Hsp110 ATP酶活性的影响尚不清楚，且尚未测量Hsp110与肽的亲和力。我们现在报道一种与酵母Hsp110 Sse1p结合的肽，其解离常数（K(D)）约为2 nM。令人惊讶的是，这种肽的结合未能刺激Sse1p的ATP水解。此外，一种与Hsp70结合的肽无法与Sse1p结合，这表明Hsp70和Hsp110具有部分不同的肽识别基序。
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