SrasV1, PubMed, Curation, bibRecord, 000916

SARS coronavirus protein nsp1 disrupts localization of Nup93 from the nuclear pore complex.

Identifieur interne : 000916 ( PubMed/Curation ); précédent : 000915; suivant : 000917

SARS coronavirus protein nsp1 disrupts localization of Nup93 from the nuclear pore complex.

Auteurs : Garret N. Gomez [États-Unis] ; Fareeha Abrar [États-Unis] ; Maya P. Dodhia [États-Unis] ; Fabiola G. Gonzalez [États-Unis] ; Anita Nag [États-Unis]

Source :

Biochemistry and cell biology = Biochimie et biologie cellulaire [ 1208-6002 ] ; 2019.

RBID : pubmed:30943371

Descripteurs français

English descriptors

KwdEn :
- Cells, Cultured, Cytoplasm (genetics), Cytoplasm (metabolism), HEK293 Cells, Humans, Nuclear Pore (genetics), Nuclear Pore (metabolism), Nuclear Pore Complex Proteins (genetics), Nuclear Pore Complex Proteins (metabolism), Phosphoproteins (genetics), Phosphoproteins (metabolism), RNA Replicase (genetics), RNA Replicase (metabolism), RNA-Binding Proteins (genetics), RNA-Binding Proteins (metabolism), Viral Nonstructural Proteins (genetics), Viral Nonstructural Proteins (metabolism).
MESH :
- chemical , genetics : Nuclear Pore Complex Proteins, Phosphoproteins, RNA Replicase, RNA-Binding Proteins, Viral Nonstructural Proteins.
- genetics : Cytoplasm, Nuclear Pore.
- metabolism : Cytoplasm, Nuclear Pore, Nuclear Pore Complex Proteins, Phosphoproteins, RNA Replicase, RNA-Binding Proteins, Viral Nonstructural Proteins.
- Cells, Cultured, HEK293 Cells, Humans.

Abstract

Severe acute respiratory syndrome coronavirus nonstructural protein 1 (nsp1) is a key factor in virus-induced down-regulation of host gene expression. In infected cells, nsp1 engages in a multipronged mechanism to inhibit host gene expression by binding to the 40S ribosome to block the assembly of translationally competent ribosome, and then inducing endonucleolytic cleavage and the degradation of host mRNAs. Here, we report a previously undetected mechanism by which nsp1 exploits the nuclear pore complex and disrupts the nuclear-cytoplasmic transport of biomolecules. We identified members of the nuclear pore complex from the nsp1-associated protein assembly and found that the expression of nsp1 in HEK cells disrupts Nup93 localization around the nuclear envelope without triggering proteolytic degradation, while the nuclear lamina remains unperturbed. Consistent with its role in host shutoff, nsp1 alters the nuclear-cytoplasmic distribution of an RNA binding protein, nucleolin. Our results suggest that nsp1, alone, can regulate multiple steps of gene expression including nuclear-cytoplasmic transport.

DOI: 10.1139/bcb-2018-0394
PubMed: 30943371

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Le document en format XML

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<term>Cytoplasm (metabolism)</term>
<term>HEK293 Cells</term>
<term>Humans</term>
<term>Nuclear Pore (genetics)</term>
<term>Nuclear Pore (metabolism)</term>
<term>Nuclear Pore Complex Proteins (genetics)</term>
<term>Nuclear Pore Complex Proteins (metabolism)</term>
<term>Phosphoproteins (genetics)</term>
<term>Phosphoproteins (metabolism)</term>
<term>RNA Replicase (genetics)</term>
<term>RNA Replicase (metabolism)</term>
<term>RNA-Binding Proteins (genetics)</term>
<term>RNA-Binding Proteins (metabolism)</term>
<term>Viral Nonstructural Proteins (genetics)</term>
<term>Viral Nonstructural Proteins (metabolism)</term>
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<term>Cellules cultivées</term>
<term>Complexe protéique du pore nucléaire (génétique)</term>
<term>Complexe protéique du pore nucléaire (métabolisme)</term>
<term>Cytoplasme (génétique)</term>
<term>Cytoplasme (métabolisme)</term>
<term>Humains</term>
<term>Phosphoprotéines (génétique)</term>
<term>Phosphoprotéines (métabolisme)</term>
<term>Pore nucléaire (génétique)</term>
<term>Pore nucléaire (métabolisme)</term>
<term>Protéines de liaison à l'ARN (génétique)</term>
<term>Protéines de liaison à l'ARN (métabolisme)</term>
<term>Protéines virales non structurales (génétique)</term>
<term>Protéines virales non structurales (métabolisme)</term>
<term>RNA replicase (génétique)</term>
<term>RNA replicase (métabolisme)</term>
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<term>Phosphoproteins</term>
<term>RNA Replicase</term>
<term>RNA-Binding Proteins</term>
<term>Viral Nonstructural Proteins</term>
</keywords>
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<term>Pore nucléaire</term>
<term>Protéines de liaison à l'ARN</term>
<term>Protéines virales non structurales</term>
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<term>RNA Replicase</term>
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<term>Phosphoprotéines</term>
<term>Pore nucléaire</term>
<term>Protéines de liaison à l'ARN</term>
<term>Protéines virales non structurales</term>
<term>RNA replicase</term>
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<term>HEK293 Cells</term>
<term>Humans</term>
</keywords>
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<front><div type="abstract" xml:lang="en">Severe acute respiratory syndrome coronavirus nonstructural protein 1 (nsp1) is a key factor in virus-induced down-regulation of host gene expression. In infected cells, nsp1 engages in a multipronged mechanism to inhibit host gene expression by binding to the 40S ribosome to block the assembly of translationally competent ribosome, and then inducing endonucleolytic cleavage and the degradation of host mRNAs. Here, we report a previously undetected mechanism by which nsp1 exploits the nuclear pore complex and disrupts the nuclear-cytoplasmic transport of biomolecules. We identified members of the nuclear pore complex from the nsp1-associated protein assembly and found that the expression of nsp1 in HEK cells disrupts Nup93 localization around the nuclear envelope without triggering proteolytic degradation, while the nuclear lamina remains unperturbed. Consistent with its role in host shutoff, nsp1 alters the nuclear-cytoplasmic distribution of an RNA binding protein, nucleolin. Our results suggest that nsp1, alone, can regulate multiple steps of gene expression including nuclear-cytoplasmic transport.</div>
</front>
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<Abstract><AbstractText>Severe acute respiratory syndrome coronavirus nonstructural protein 1 (nsp1) is a key factor in virus-induced down-regulation of host gene expression. In infected cells, nsp1 engages in a multipronged mechanism to inhibit host gene expression by binding to the 40S ribosome to block the assembly of translationally competent ribosome, and then inducing endonucleolytic cleavage and the degradation of host mRNAs. Here, we report a previously undetected mechanism by which nsp1 exploits the nuclear pore complex and disrupts the nuclear-cytoplasmic transport of biomolecules. We identified members of the nuclear pore complex from the nsp1-associated protein assembly and found that the expression of nsp1 in HEK cells disrupts Nup93 localization around the nuclear envelope without triggering proteolytic degradation, while the nuclear lamina remains unperturbed. Consistent with its role in host shutoff, nsp1 alters the nuclear-cytoplasmic distribution of an RNA binding protein, nucleolin. Our results suggest that nsp1, alone, can regulate multiple steps of gene expression including nuclear-cytoplasmic transport.</AbstractText>
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</AffiliationInfo>
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</AffiliationInfo>
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</AffiliationInfo>
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</AffiliationInfo>
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</AffiliationInfo>
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<Language>eng</Language>
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<NameOfSubstance UI="C508154">Nup93 protein, human</NameOfSubstance>
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<MeshHeading><DescriptorName UI="D016601" MajorTopicYN="N">RNA-Binding Proteins</DescriptorName>
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<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
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<Keyword MajorTopicYN="Y">SARS-CoV</Keyword>
<Keyword MajorTopicYN="Y">SLN</Keyword>
<Keyword MajorTopicYN="Y">SRAS-CoV</Keyword>
<Keyword MajorTopicYN="Y">complexe des pores nucléaires</Keyword>
<Keyword MajorTopicYN="Y">immunofluorescence</Keyword>
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<Month>4</Month>
<Day>4</Day>
<Hour>6</Hour>
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SARS coronavirus protein nsp1 disrupts localization of Nup93 from the nuclear pore complex.

SARS coronavirus protein nsp1 disrupts localization of Nup93 from the nuclear pore complex.

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