Import of adenovirus DNA involves the nuclear pore complex receptor CAN/Nup214 and histone H1

Trotman, L. C., Mosberger, N., Fornerod, M., Stidwill, R. P., Greber, U. F. (2001) Import of adenovirus DNA involves the nuclear pore complex receptor CAN/Nup214 and histone H1. Nature Cell Biology, 3 (12). pp. 1092-1100. ISSN 14657392 (ISSN)

DOI: 10.1038/ncb1201-1092


Adenovirus type 2 (Ad2) imports its DNA genome through the nuclear pore complex (NPC) of cells in interphase for viral production. Here we identify the NPC-filament protein CAN/Nup214 as a docking site for incoming Ad2 capsids. Binding to CAN is independent of cytosolic factors. Capsids disassemble at NPCs to free their DNA for import. This process requires binding of nuclear histone H1 to the stably docked capsids and involves H1-import factors, restricting this irreversible process to the proximity of the nucleus. Our results provide a molecular mechanism for disassembly of Ad2 and reveal an unexpected function of histone H1 in virus-mediated DNA import.

Item Type: Paper
Additional Information: PubMed ID: 11781571
Uncontrolled Keywords: cell nucleus receptor histone H1 nucleoprotein virus DNA Adenovirus 2 animal cell article complex formation controlled study cytosol human human cell interphase nonhuman priority journal protein binding rat virogenesis virus capsid virus genome Active Transport, Cell Nucleus Adenoviridae alpha Karyopherins Amino Acid Sequence Antibodies beta Karyopherins Capsid Capsid Proteins DNA, Viral Histones Humans Lung Neoplasms Molecular Sequence Data Nuclear Pore Nuclear Pore Complex Proteins Tumor Cells Cultured Animalia DNA viruses Human adenovirus type 2 Miridae
Subjects: bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > histone
organism description > virus
CSHL Authors:
Communities: CSHL labs > Trotman lab
Depositing User: Brian Soldo
Date: 2001
Date Deposited: 23 Mar 2012 16:08
Last Modified: 08 May 2013 16:49
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