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Tsuiyi Peng - One of the best experts on this subject based on the ideXlab platform.
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phosphorylation of the arginine serine dipeptide rich motif of the severe acute respiratory syndrome coronavirus Nucleocapsid Protein modulates its multimerization translation inhibitory activity and cellular localization
FEBS Journal, 2008Co-Authors: Tsuiyi Peng, Woanyuh TarnAbstract:Coronavirus Nucleocapsid Protein is abundant in infected cells and participates in viral RNA replication and transcription. The central domain of the Nucleocapsid Protein contains several arginine/serine (RS) dipeptides, the biological significance of which has not been well investigated. In the present study, we demonstrate that the severe acute respiratory syndrome coronavirus Nucleocapsid Protein is phosphorylated primarily within the RS-rich region in cells and by SR Protein kinase 1 in vitro. The Nucleocapsid Protein could suppress translation and its RS motif is essential for such an activity. Moreover, phosphorylation of the RS motif could modulate the translation inhibitory activity of the Nucleocapsid Protein. We further found that RS motif phosphorylation did not significantly affect RNA binding of the Nucleocapsid Protein but impaired its multimerization ability. We observed that the Nucleocapsid Protein could translocate to cytoplasmic stress granules in response to cellular stress. Deletion or mutations of the RS motif enhanced stress granule localization of the Nucleocapsid Protein, whereas overexpression of SR Protein kinase 1 inhibited Nucleocapsid Protein localization to stress granules. The Nucleocapsid Protein lacking the RS motif formed high-order RNP complexes, which may also account for its enhanced stress granule localization. Taken together, phosphorylation of the severe acute respiratory syndrome-CoV Nucleocapsid Protein modulates its activity in translation control and also interferes with its oligomerization and aggregation in stress granules.
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Phosphorylation of the arginine/serine dipeptide-rich motif of the severe acute respiratory syndrome coronavirus Nucleocapsid Protein modulates its multimerization, translation inhibitory activity and cellular localization.
The FEBS journal, 2008Co-Authors: Tsuiyi Peng, Kuan-rong Lee, Woanyuh TarnAbstract:Coronavirus Nucleocapsid Protein is abundant in infected cells and participates in viral RNA replication and transcription. The central domain of the Nucleocapsid Protein contains several arginine/serine (RS) dipeptides, the biological significance of which has not been well investigated. In the present study, we demonstrate that the severe acute respiratory syndrome coronavirus Nucleocapsid Protein is phosphorylated primarily within the RS-rich region in cells and by SR Protein kinase 1 in vitro. The Nucleocapsid Protein could suppress translation and its RS motif is essential for such an activity. Moreover, phosphorylation of the RS motif could modulate the translation inhibitory activity of the Nucleocapsid Protein. We further found that RS motif phosphorylation did not significantly affect RNA binding of the Nucleocapsid Protein but impaired its multimerization ability. We observed that the Nucleocapsid Protein could translocate to cytoplasmic stress granules in response to cellular stress. Deletion or mutations of the RS motif enhanced stress granule localization of the Nucleocapsid Protein, whereas overexpression of SR Protein kinase 1 inhibited Nucleocapsid Protein localization to stress granules. The Nucleocapsid Protein lacking the RS motif formed high-order RNP complexes, which may also account for its enhanced stress granule localization. Taken together, phosphorylation of the severe acute respiratory syndrome-CoV Nucleocapsid Protein modulates its activity in translation control and also interferes with its oligomerization and aggregation in stress granules.
Woanyuh Tarn - One of the best experts on this subject based on the ideXlab platform.
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phosphorylation of the arginine serine dipeptide rich motif of the severe acute respiratory syndrome coronavirus Nucleocapsid Protein modulates its multimerization translation inhibitory activity and cellular localization
FEBS Journal, 2008Co-Authors: Tsuiyi Peng, Woanyuh TarnAbstract:Coronavirus Nucleocapsid Protein is abundant in infected cells and participates in viral RNA replication and transcription. The central domain of the Nucleocapsid Protein contains several arginine/serine (RS) dipeptides, the biological significance of which has not been well investigated. In the present study, we demonstrate that the severe acute respiratory syndrome coronavirus Nucleocapsid Protein is phosphorylated primarily within the RS-rich region in cells and by SR Protein kinase 1 in vitro. The Nucleocapsid Protein could suppress translation and its RS motif is essential for such an activity. Moreover, phosphorylation of the RS motif could modulate the translation inhibitory activity of the Nucleocapsid Protein. We further found that RS motif phosphorylation did not significantly affect RNA binding of the Nucleocapsid Protein but impaired its multimerization ability. We observed that the Nucleocapsid Protein could translocate to cytoplasmic stress granules in response to cellular stress. Deletion or mutations of the RS motif enhanced stress granule localization of the Nucleocapsid Protein, whereas overexpression of SR Protein kinase 1 inhibited Nucleocapsid Protein localization to stress granules. The Nucleocapsid Protein lacking the RS motif formed high-order RNP complexes, which may also account for its enhanced stress granule localization. Taken together, phosphorylation of the severe acute respiratory syndrome-CoV Nucleocapsid Protein modulates its activity in translation control and also interferes with its oligomerization and aggregation in stress granules.
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Phosphorylation of the arginine/serine dipeptide-rich motif of the severe acute respiratory syndrome coronavirus Nucleocapsid Protein modulates its multimerization, translation inhibitory activity and cellular localization.
The FEBS journal, 2008Co-Authors: Tsuiyi Peng, Kuan-rong Lee, Woanyuh TarnAbstract:Coronavirus Nucleocapsid Protein is abundant in infected cells and participates in viral RNA replication and transcription. The central domain of the Nucleocapsid Protein contains several arginine/serine (RS) dipeptides, the biological significance of which has not been well investigated. In the present study, we demonstrate that the severe acute respiratory syndrome coronavirus Nucleocapsid Protein is phosphorylated primarily within the RS-rich region in cells and by SR Protein kinase 1 in vitro. The Nucleocapsid Protein could suppress translation and its RS motif is essential for such an activity. Moreover, phosphorylation of the RS motif could modulate the translation inhibitory activity of the Nucleocapsid Protein. We further found that RS motif phosphorylation did not significantly affect RNA binding of the Nucleocapsid Protein but impaired its multimerization ability. We observed that the Nucleocapsid Protein could translocate to cytoplasmic stress granules in response to cellular stress. Deletion or mutations of the RS motif enhanced stress granule localization of the Nucleocapsid Protein, whereas overexpression of SR Protein kinase 1 inhibited Nucleocapsid Protein localization to stress granules. The Nucleocapsid Protein lacking the RS motif formed high-order RNP complexes, which may also account for its enhanced stress granule localization. Taken together, phosphorylation of the severe acute respiratory syndrome-CoV Nucleocapsid Protein modulates its activity in translation control and also interferes with its oligomerization and aggregation in stress granules.
Brenda G. Hogue - One of the best experts on this subject based on the ideXlab platform.
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Coronavirus Nucleocapsid Protein
Advances in Experimental Medicine and Biology, 1998Co-Authors: Raymond Cologna, Brenda G. HogueAbstract:The Coronavirus Nucleocapsid Protein (N) is involved in encapsidation and packaging of viral RNA. In this study we investigated the ability of the bovine Coronavirus (BCV) N Protein to interact with RNA. Histidine-tagged BCV N (his-N) Protein was expressed in bacteria. A filter binding assay was established to quantitatively measure the binding efficiency of purified his-N to different RNAs. The results indicate that bacterially expressed N bound both BCV and mouse hepatitis Coronavirus (MHV) RNAs. Binding to in vitro generated BCV and MHV RNA transcripts was significantly higher than binding to a non-coronavirus RNA. Similar binding efficiencies were measured for a BCV defective genome, pDrep, and a transcript that contained the MHV packaging signal. Interestingly, the entire MHV DI, pMIDI-C, was bound at a higher efficiency than the packaging signal alone. This is one of the first reports to show that N interacts with the MHV packaging signal.
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Coronavirus Nucleocapsid Protein: RNA interactions
Advances in Experimental Medicine and Biology, 1998Co-Authors: Raymond Cologna, Brenda G. HogueAbstract:The coronavirus Nucleocapsid Protein (N) is involved in encapsidation and packaging of viral RNA. In this study we investigated the ability of the bovine coronavirus (BCV) N Protein to interact with RNA. Histidine-tagged BCV N (his-N) Protein was expressed in bacteria. A filter binding assay was established to quantitatively measure the binding efficiency of purified his-N to different RNAs. The results indicate that bacterially expressed N bound both BCV and mouse hepatitis coronavirus (MHV) RNAs. Binding to in vitro generated BCV and MHV RNA transcripts was significantly higher than binding to a non-coronavirus RNA. Similar binding efficiencies were measured for a BCV defective genome, pDrep, and a transcript that contained the MHV packaging signal. Interestingly, the entire MHV Dr, pMIDI-C, was bound at a higher efficiency than the packaging signal alone. This is one of the first reports to show that N interacts with the MHV packaging signal.
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Bovine Coronavirus Nucleocapsid Protein Processing and Assembly
Advances in Experimental Medicine and Biology, 1995Co-Authors: Brenda G. HogueAbstract:The coronavirus Nucleocapsid Protein (N) encapsidates the genomic RNA to form a helical Nucleocapsid. The requirements for coronavirus Nucleocapsid assembly are being studied. Two forms (∼50 kDa and 55 kDa) of the bovine coronavirus (BCV) N Protein were detected in infected cells. However, only one form, a 50 kDa species, was detected in extracellular virions. After treatment with calf intestinal alkaline phosphatase (CIAP), the 55 kDa intracellular form increased in mobility to comigrate with the 50 kDa form; whereas, the 50 kDa intracellular species and N from extracellular virions was not sensitive to CIAP treatment. The data indicate that specificity exists with regard to assembly of N into the mature virion. The data suggests that processing of N may take place during assembly of either Nucleocapsids or virions and that the processing may be a dephosphorylation event.
Taihuang Huang - One of the best experts on this subject based on the ideXlab platform.
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structure of the sars coronavirus Nucleocapsid Protein rna binding dimerization domain suggests a mechanism for helical packaging of viral rna
Journal of Molecular Biology, 2007Co-Authors: Chunyuan Chen, Chung Ke Chang, Yiwei Chang, Shih Che Sue, Hsin I Bai, Lilianty Riang, Chwandeng Hsiao, Taihuang HuangAbstract:Coronavirus Nucleocapsid Proteins are basic Proteins that encapsulate viral genomic RNA to form part of the virus structure. The Nucleocapsid Protein of SARS-CoV is highly antigenic and associated with several host-cell interactions. Our previous studies using nuclear magnetic resonance revealed the domain organization of the SARS-CoV Nucleocapsid Protein. RNA has been shown to bind to the N-terminal domain (NTD), although recently the C-terminal half of the Protein has also been implicated in RNA binding. Here, we report that the C-terminal domain (CTD), spanning residues 248-365 (NP248-365), had stronger nucleic acid-binding activity than the NTD. To determine the molecular basis of this activity, we have also solved the crystal structure of the NP248-365 region. Residues 248-280 form a positively charged groove similar to that found in the infectious bronchitis virus (IBV) Nucleocapsid Protein. Furthermore, the positively charged surface area is larger in the SARS-CoV construct than in the IBV. Interactions between residues 248-280 and the rest of the molecule also stabilize the formation of an octamer in the asymmetric unit. Packing of the octamers in the crystal forms two parallel, basic helical grooves, which may be oligonucleotide attachment sites, and suggests a mechanism for helical RNA packaging in the virus.
Yan Yan - One of the best experts on this subject based on the ideXlab platform.
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crystal structure of sars cov 2 Nucleocapsid Protein rna binding domain reveals potential unique drug targeting sites
Acta Pharmaceutica Sinica B, 2020Co-Authors: Sisi Kang, Mei Yang, Zhongsi Hong, Liping Zhang, Zhaoxia Huang, Xiaoxue Chen, Ziliang Zhou, Zhechong Zhou, Qiuyue Chen, Yan YanAbstract:Abstract The outbreak of coronavirus disease (COVID-19) caused by SARS-CoV-2 virus continually lead to worldwide human infections and deaths. Currently, there is no specific viral Protein-targeted therapeutics. Viral Nucleocapsid Protein is a potential antiviral drug target, serving multiple critical functions during the viral life cycle. However, the structural information of SARS-CoV-2 Nucleocapsid Protein remains unclear. Herein, we have determined the 2.7 A crystal structure of the N-terminal RNA binding domain of SARS-CoV-2 Nucleocapsid Protein. Although the overall structure is similar as other reported coronavirus Nucleocapsid Protein N-terminal domain, the surface electrostatic potential characteristics between them are distinct. Further comparison with mild virus type HCoV-OC43 equivalent domain demonstrates a unique potential RNA binding pocket alongside the β-sheet core. Complemented by in vitro binding studies, our data provide several atomic resolution features of SARS-CoV-2 Nucleocapsid Protein N-terminal domain, guiding the design of novel antiviral agents specific targeting to SARS-CoV-2.
