SARS coronavirus protein nsp1 disrupts localization of Nup93 from the nuclear pore complex.
Identifieur interne : 000A98 ( Main/Exploration ); précédent : 000A97; suivant : 000A99SARS 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.
Descripteurs français
- KwdFr :
- Cellules HEK293, Cellules cultivées, Complexe protéique du pore nucléaire (génétique), Complexe protéique du pore nucléaire (métabolisme), Cytoplasme (génétique), Cytoplasme (métabolisme), Humains, Phosphoprotéines (génétique), Phosphoprotéines (métabolisme), Pore nucléaire (génétique), Pore nucléaire (métabolisme), Protéines de liaison à l'ARN (génétique), Protéines de liaison à l'ARN (métabolisme), Protéines virales non structurales (génétique), Protéines virales non structurales (métabolisme), RNA replicase (génétique), RNA replicase (métabolisme).
- MESH :
- génétique : Complexe protéique du pore nucléaire, Cytoplasme, Phosphoprotéines, Pore nucléaire, Protéines de liaison à l'ARN, Protéines virales non structurales, RNA replicase.
- métabolisme : Complexe protéique du pore nucléaire, Cytoplasme, Phosphoprotéines, Pore nucléaire, Protéines de liaison à l'ARN, Protéines virales non structurales, RNA replicase.
- Cellules HEK293, Cellules cultivées, Humains.
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
Affiliations:
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Le document en format XML
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Gomez</name><affiliation wicri:level="2"><nlm:affiliation>Furman University, 3300 Poinsett Highway, Greenville, SC 29613, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Furman University, 3300 Poinsett Highway, Greenville, SC 29613</wicri:regionArea><placeName><region type="state">Caroline du Sud</region></placeName></affiliation></author><author><name sortKey="Abrar, Fareeha" sort="Abrar, Fareeha" uniqKey="Abrar F" first="Fareeha" last="Abrar">Fareeha Abrar</name><affiliation wicri:level="2"><nlm:affiliation>Furman University, 3300 Poinsett Highway, Greenville, SC 29613, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Furman University, 3300 Poinsett Highway, Greenville, SC 29613</wicri:regionArea><placeName><region type="state">Caroline du Sud</region></placeName></affiliation></author><author><name sortKey="Dodhia, Maya P" sort="Dodhia, Maya P" uniqKey="Dodhia M" first="Maya P" last="Dodhia">Maya P. 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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></TEI><affiliations><list><country><li>États-Unis</li></country><region><li>Caroline du Sud</li></region></list><tree><country name="États-Unis"><region name="Caroline du Sud"><name sortKey="Gomez, Garret N" sort="Gomez, Garret N" uniqKey="Gomez G" first="Garret N" last="Gomez">Garret N. Gomez</name></region><name sortKey="Abrar, Fareeha" sort="Abrar, Fareeha" uniqKey="Abrar F" first="Fareeha" last="Abrar">Fareeha Abrar</name><name sortKey="Dodhia, Maya P" sort="Dodhia, Maya P" uniqKey="Dodhia M" first="Maya P" last="Dodhia">Maya P. Dodhia</name><name sortKey="Gonzalez, Fabiola G" sort="Gonzalez, Fabiola G" uniqKey="Gonzalez F" first="Fabiola G" last="Gonzalez">Fabiola G. Gonzalez</name><name sortKey="Nag, Anita" sort="Nag, Anita" uniqKey="Nag A" first="Anita" last="Nag">Anita Nag</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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