Elucidation of the stability and functional regions of the human coronavirus OC43 nucleocapsid protein.
Identifieur interne : 002B28 ( Main/Exploration ); précédent : 002B27; suivant : 002B29Elucidation of the stability and functional regions of the human coronavirus OC43 nucleocapsid protein.
Auteurs : Chun-Yu Huang [Taïwan] ; Yen-Lan Hsu ; Wan-Ling Chiang ; Ming-Hon HouSource :
- Protein science : a publication of the Protein Society [ 1469-896X ] ; 2009.
Descripteurs français
- KwdFr :
- Acides nucléiques (métabolisme), Coronavirus humain OC43 (), Dichroïsme circulaire, Glutaraldéhyde (), Humains, Multimérisation de protéines, Protéines de liaison à l'ARN (), Protéines de liaison à l'ARN (métabolisme), Protéines nucléocapside (), Protéines nucléocapside (métabolisme), Protéines recombinantes (), Protéines recombinantes (métabolisme), Sites de fixation, Spectrométrie de fluorescence, Stabilité protéique, Urée ().
- MESH :
- métabolisme : Acides nucléiques, Protéines de liaison à l'ARN, Protéines nucléocapside, Protéines recombinantes.
- Coronavirus humain OC43, Dichroïsme circulaire, Glutaraldéhyde, Humains, Multimérisation de protéines, Protéines de liaison à l'ARN, Protéines nucléocapside, Protéines recombinantes, Sites de fixation, Spectrométrie de fluorescence, Stabilité protéique, Urée.
English descriptors
- KwdEn :
- Binding Sites, Circular Dichroism, Coronavirus OC43, Human (chemistry), Glutaral (chemistry), Humans, Nucleic Acids (metabolism), Nucleocapsid Proteins (chemistry), Nucleocapsid Proteins (metabolism), Protein Multimerization, Protein Stability, RNA-Binding Proteins (chemistry), RNA-Binding Proteins (metabolism), Recombinant Proteins (chemistry), Recombinant Proteins (metabolism), Spectrometry, Fluorescence, Urea (chemistry).
- MESH :
- chemical , chemistry : Glutaral, Nucleocapsid Proteins, RNA-Binding Proteins, Recombinant Proteins, Urea.
- chemistry : Coronavirus OC43, Human.
- chemical , metabolism : Nucleic Acids, Nucleocapsid Proteins, RNA-Binding Proteins, Recombinant Proteins.
- Binding Sites, Circular Dichroism, Humans, Protein Multimerization, Protein Stability, Spectrometry, Fluorescence.
Abstract
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.
DOI: 10.1002/pro.225
PubMed: 19691129
Affiliations:
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Le document en format XML
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<front><div type="abstract" xml:lang="en">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.</div>
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