RNA Binding Sensitivity of Nonstructural Protein 8 Revealed by Small-Angle Neutron Scattering and Alphafold2 Prediction
Xin Jiang, Jinxin Xu, Zhenyu Liao, Na Wang, Taisen Zuo, Changli Ma, Hanqiu Jiang, Yubin Ke, He Cheng, Howard Wang, Jinkui Zhao, Jun Fan, Jinsong Liu, Xiangqiang Chu
TL;DR
This study reveals how a flexible protein from SARS-CoV-2 changes structure to interact with RNA, aiding virus replication.
Contribution
The study identifies the RNA binding sensitivity of nsp8 tetramers through neutron scattering and AlphaFold2 predictions.
Findings
The nsp8 tetramer has a more exposed core domain and lower thermal stability.
The exposed core domain increases RNA sensitivity and structural adaptability.
Structural differences between nsp8 dimers and tetramers are linked to RNA replication.
Abstract
The flexible structure enables nonstructural protein 8 (nsp8) to respond quickly to environmental changes, which are essential for RNA replication and transcription of SARS-CoV-2. In this work, small-angle neutron scattering and AlphaFold2 prediction were applied to characterize the structural change of SARS-CoV-2 nsp8 dimers and tetramers. The results demonstrated that the nsp8 tetramer with a more exposed core domain shows a low thermal stability. The exposed core domain increases its sensitivity to RNA and adapts its structure to interact with RNA. Our work reveals the structural difference between the two forms of SARS-CoV-2 nsp8s in the RNA synthesis process, which partly elucidates the molecular mechanism behind RNA replication of the RNA virus.
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Taxonomy
TopicsEnzyme Structure and Function · RNA and protein synthesis mechanisms · Protein Structure and Dynamics