Your browser doesn't support javascript.
loading
Show: 20 | 50 | 100
Results 1 - 1 de 1
Filter
Add more filters










Database
Language
Publication year range
1.
Nat Cell Biol ; 3(12): 1092-100, 2001 Dec.
Article in English | MEDLINE | ID: mdl-11781571

ABSTRACT

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.


Subject(s)
Adenoviridae/genetics , Capsid Proteins , DNA, Viral/pharmacokinetics , Histones/metabolism , Nuclear Pore Complex Proteins/metabolism , Nuclear Pore/metabolism , Active Transport, Cell Nucleus/physiology , Amino Acid Sequence , Antibodies/pharmacology , Capsid/genetics , Capsid/immunology , Capsid/metabolism , Histones/immunology , Humans , Lung Neoplasms , Molecular Sequence Data , Nuclear Pore Complex Proteins/immunology , Protein Binding/physiology , Tumor Cells, Cultured , alpha Karyopherins/metabolism , beta Karyopherins/metabolism
SELECTION OF CITATIONS
SEARCH DETAIL
...