Patel Jayneil R, Xu Yingqi, Capitini Claudia, Chiti Fabrizio, De Simone Alfonso
Department of Life Sciences, Imperial College London, South Kensington, London, SW72AZ, UK.
Section of Biochemistry, Department of Experimental and Clinical Biomedical Sciences, University of Florence, Viale Morgagni 50, 50134, Firenze, Italy.
Biomol NMR Assign. 2018 Oct;12(2):273-277. doi: 10.1007/s12104-018-9822-7. Epub 2018 May 21.
The HypF protein is involved in the maturation and regulation of hydrogenases. The N-terminal domain of HypF (HypF-N) has served as a key model system to study the pathways of protein amyloid formation and the nature of the toxicity of pre-fibrilar protein oligomers. This domain can aggregate into two forms of oligomers having significantly different toxic effects when added to neuronal cultures. Here, NMR assignments of HypF-N backbone resonances are presented in its native state and under the conditions favouring the formation of toxic and non-toxic oligomers. The analyses of chemical shifts provide insights into the protein conformational state and the possible pathways leading to the formation of different types of oligomers.
HypF蛋白参与氢化酶的成熟和调节。HypF的N端结构域（HypF-N）已成为研究蛋白质淀粉样形成途径和纤维前体蛋白寡聚体毒性本质的关键模型系统。当添加到神经元培养物中时，该结构域可聚集成两种具有显著不同毒性作用的寡聚体形式。本文给出了HypF-N主链共振在其天然状态以及有利于形成有毒和无毒寡聚体的条件下的核磁共振归属。化学位移分析为蛋白质构象状态以及导致形成不同类型寡聚体的可能途径提供了见解。
