Structure, Function, Folding, and Aggregation of a Neuroferritinopathy-Related Ferritin Variant

Kuwata Takumi; Okada Yuta; Yamamoto Tomoki; Sato Daisuke; Fujiwara Kazuo; Fukumura Takuma; Ikeguchi Masamichi

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Structure, Function, Folding, and Aggregation of a Neuroferritinopathy-Related Ferritin Variant

机译：神经烧制症相关铁蛋白变体的结构，功能，折叠和聚集

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Neuroferritinopathy is a rare, adult-onset, dominantly inherited movement disorder caused by mutations in the ferritin gene. A ferritin light-chain variant related to neuroferritinopathy, in which alanine 96 is replaced with threonine (A96T), was expressed in Escherichia coli, purified, and characterized. The circular dichroism, analytical ultra-centrifugation, and small-angle X-ray scattering studies have shown that both the subunit structure and the assembly of A96T are the same as those of wild-type human ferritin light chain (HuFTL). The iron-incorporation ability was also comparable to that of HuFTL. Although the structural stability against heat, acid, and denaturant was reduced, the structure was sufficiently stable under physiological conditions. The most remarkable defects observed for A96T were a lower refolding efficiency and stronger propensity to aggregate. The possible relationship between folding deficiency and disease is discussed.

机译：神经烧制素病患者是由铁蛋白基因突变引起的罕见的成人发作，其主要遗传的运动障碍。与神经烧烤素相关的铁蛋白轻链变体，其中丙氨酸96被苏氨酸（A96T）替换，在大肠杆菌中表达，纯化和表征。圆形二色性，分析超离心和小角X射线散射研究表明，亚基结构和A96T的组装都与野生型人铁蛋白轻链（HUFT1）的组装相同。铁掺入能力也与huftl的能力相当。虽然减少了对热，酸和变性剂的结构稳定性，但在生理条件下该结构足够稳定。对于A96T观察到的最显着的缺陷是降低的重叠效率和更强的聚集倾向。讨论了折叠缺乏和疾病之间的可能关系。

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《Biochemistry》 |2019年第18期|共8页
作者
Kuwata Takumi; Okada Yuta; Yamamoto Tomoki; Sato Daisuke; Fujiwara Kazuo; Fukumura Takuma; Ikeguchi Masamichi;
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Soka Univ Dept Bioinformat 1-236 Tangi Machi Hachioji Tokyo 1928577 Japan;

Soka Univ Dept Bioinformat 1-236 Tangi Machi Hachioji Tokyo 1928577 Japan;

Soka Univ Dept Bioinformat 1-236 Tangi Machi Hachioji Tokyo 1928577 Japan;

Soka Univ Dept Bioinformat 1-236 Tangi Machi Hachioji Tokyo 1928577 Japan;

Soka Univ Dept Bioinformat 1-236 Tangi Machi Hachioji Tokyo 1928577 Japan;

JEOL Ltd EM Res &

Dev Dept 3-1-2 Musashino Akishima Tokyo 1968558 Japan;

Soka Univ Dept Bioinformat 1-236 Tangi Machi Hachioji Tokyo 1928577 Japan;

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正文语种 eng
中图分类生物化学;
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专利

1. Structure, Function, Folding, and Aggregation of a Neuroferritinopathy-Related Ferritin Variant [J] . Kuwata Takumi, Okada Yuta, Yamamoto Tomoki, Biochemistry . 2019,第18期

机译：神经烧制症相关铁蛋白变体的结构，功能，折叠和聚集
2. Characterization of the structure and function of W --> F WW domain variants: identification of a natively unfolded protein that folds upon ligand binding. [J] . Koepf EK, Petrassi HM, Ratnaswamy G, Biochemistry . 1999,第43期

机译：W-> F WW域变体的结构和功能的表征：鉴定在配体结合后折叠的天然未折叠蛋白。
3. Aggregation properties the controlling roles of Trp60 and Trp95 in beta(2)-microglobulin function, folding and amyloid aggregation properties [J] . Esposito G, Ricagno S, Corazza A, Journal of Molecular Biology . 2008,第4期

机译：聚集特性Trp60和Trp95在beta（2）-微球蛋白功能，折叠和淀粉样蛋白聚集特性中的控制作用
4. Morphological Bilateral Filtering and Spatially-Variant Adaptive Structuring Functions [C] . Jesus Angulo Mathematical morphology and its applications to image and signal processing . 2011

机译：形态学双边过滤和空间变异自适应结构函数
5. Alpha-synuclein sequence variants: Secondary structure formation and aggregation. [D] . Kessler, Jeffrey Charles. 2004

机译：α-突触核蛋白序列变体：二级结构的形成和聚集。
6. Crystal Structure of Plant Ferritin Reveals a Novel Metal Binding Site That Functions as a Transit Site for Metal Transfer in Ferritin [O] . Taro Masuda, Fumiyuki Goto, Toshihiro Yoshihara, 2010

机译：植物铁蛋白的晶体结构揭示了一种新颖的金属结合位点该位点充当铁蛋白中金属转移的转运位点
7. Cryo-EM structures and functional characterization of homo- and heteropolymers of human ferritin variants [O] . Jose Irimia-Dominguez, Chen Sun, Kunpeng Li, 2020

机译：人铁蛋白变体均聚物和杂化聚合物的冷冻组织结构和功能表征

Structure, Function, Folding, and Aggregation of a Neuroferritinopathy-Related Ferritin Variant

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