期刊
BIOCHEMISTRY AND CELL BIOLOGY
卷 97, 期 6, 页码 758-766出版社
CANADIAN SCIENCE PUBLISHING
DOI: 10.1139/bcb-2018-0394
关键词
SARS-CoV; nsp1; Nup93; nuclear pore complex; NLS; immunofluorescence
资金
- NIH [S10 D010731]
- South Carolina Independent Schools and College Summer Fellow awards
- South Carolina INBRE Bioinformatics Pilot Project award
- National Institute of General Medical Sciences of the National Institute of Health [P20GM103499]
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.
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