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|標題:||Elucidation of the stability and functional regions of the human coronavirus OC43 nucleocapsid protein||作者:||Huang, C.Y.
|關鍵字:||human coronavirus;OC43 strain;nucleocapsid protein;Ribonucleocapsid;stability;RNA-binding regions;oligomerization domain;acute-respiratory-syndrome;infectious-bronchitis virus;mouse;hepatitis-virus;rna-binding domain;n-terminal domain;dimerization;domain;crystal-structure;leader rna;sars;transcription||Project:||Protein Science||期刊/報告no：:||Protein Science, Volume 18, Issue 11, Page(s) 2209-2218.||摘要:||
Human coronavirus OC43 (HCoV-OC43) is one of the causes of the "common cold" in human during seasons of cold weather. The primary function of the HCoV-OC43 nucleocapsid protein (N protein) is to recognize viral genomic RNA, which leads to ribonucleocapsid formation. Here, we characterized the stability and identified the functional regions of the recombinant HCoV-OC43 N protein. Circular dichroism and fluorescence measurements revealed that the HCoV-OC43 N protein is more highly ordered and stabler than the SARS-CoV N protein previously studied. Surface plasmon resonance (SPR) experiments showed that the affinity of HCoV-OC43 N protein for RNA was approximately fivefold higher than that of N protein for DNA. Moreover, we found that the HCoV-OC43 N protein contains three RNA-binding regions in its N-terminal region (residues 1-173) and central-linker region (residues 174-232 and 233-300). The binding affinities of the truncated N proteins and RNA follow the order: residues 1-173-residues 233-300 > residues 174-232. SPR experiments demonstrated that the C-terminal region (residues 301-448) of HCoV-OC43 N protein lacks RNA-binding activity, while crosslinking and gel filtration analyses revealed that the C-terminal region is mainly involved in the oligomerization of the HCoV-OC43 N protein. This study may benefit the understanding of the mechanism of HCoV-OC43 nucleocapsid formation.
|Appears in Collections:||基因體暨生物資訊學研究所|
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