Backbone 1H, 13C, and 15N chemical shift assignments for human SERF2

IF 0.8 4区 生物学 Q4 BIOPHYSICS Biomolecular NMR Assignments Pub Date : 2024-03-11 DOI:10.1007/s12104-024-10167-5
Bikash R. Sahoo, Vivekanandan Subramanian, James C.A. Bardwell
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Abstract

Human small EDRK-rich factor protein SERF2 is a cellular driver of protein amyloid formation, a process that has been linked to neurodegenerative diseases including Alzheimer’s and Parkinson’s disease. SERF2 is a 59 amino acid protein, highly charged, and well conserved whose structure and physiological function is unclear. SERF family proteins including human SERF2 have shown a tendency to form fuzzy complexes with misfolded proteins such as α-Synuclein which has been linked to Parkinson’s disease. SERF family proteins have been recently identified to bind nucleic acids, but the binding mechanism(s) remain enigmatic. Here, using multidimensional solution NMR, we report the 1H, 15N, and 13C chemical shift assignments (~ 86% of backbone resonance assignments) for human SERF2. TALOS-N predicted secondary structure of SERF2 showed three very short helices (3–4 residues long) in the N-terminal region of the protein and a long helix in the C-terminal region spanning residues 37–46 which is consistent with the helical content indicated by circular dichroism spectroscopy. Paramagnetic relaxation enhancement NMR analysis revealed that a short C-terminal region E53-K55 is in the proximity of the N-terminus. Having the backbone assignment of SERF2 allowed us to probe its interaction with α-Synuclein and to identify the residues in SERF2 binding interfaces that likely promote α-Synuclein aggregation.

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人类 SERF2 的骨架 1H、13C 和 15N 化学位移分布图
人类富含 EDRK 的小因子蛋白 SERF2 是蛋白质淀粉样蛋白形成的细胞驱动因素,这一过程与包括阿尔茨海默氏症和帕金森氏症在内的神经退行性疾病有关。SERF2 是一种 59 个氨基酸的蛋白质,带高电荷,其结构和生理功能尚不清楚。包括人类 SERF2 在内的 SERF 家族蛋白显示出与折叠错误的蛋白质(如与帕金森病有关的 α-突触核蛋白)形成模糊复合物的倾向。最近发现 SERF 家族蛋白能与核酸结合,但其结合机制仍是个谜。在这里,我们利用多维溶液核磁共振,报告了人类 SERF2 的 1H、15N 和 13C 化学位移分配(约占骨干共振分配的 86%)。TALOS-N 预测的 SERF2 二级结构显示,该蛋白的 N 端区域有三个非常短的螺旋(3-4 个残基长),C 端区域有一个长螺旋,跨越 37-46 个残基,这与圆二色性光谱显示的螺旋含量一致。顺磁弛豫增强核磁共振分析表明,短 C 端区域 E53-K55 位于 N 端附近。有了 SERF2 的骨架分配,我们就能探究它与α-突触核蛋白的相互作用,并确定 SERF2 结合界面中可能促进α-突触核蛋白聚集的残基。
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来源期刊
Biomolecular NMR Assignments
Biomolecular NMR Assignments 生物-光谱学
CiteScore
1.70
自引率
11.10%
发文量
59
审稿时长
6-12 weeks
期刊介绍: Biomolecular NMR Assignments provides a forum for publishing sequence-specific resonance assignments for proteins and nucleic acids as Assignment Notes. Chemical shifts for NMR-active nuclei in macromolecules contain detailed information on molecular conformation and properties. Publication of resonance assignments in Biomolecular NMR Assignments ensures that these data are deposited into a public database at BioMagResBank (BMRB; http://www.bmrb.wisc.edu/), where they are available to other researchers. Coverage includes proteins and nucleic acids; Assignment Notes are processed for rapid online publication and are published in biannual online editions in June and December.
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