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

Lloyd C. Trotman; Nicole Mosberger; Maarten Fornerod; Robert P. Stidwill; Urs F. Greber

doi:10.1038/ncb1201-1092

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

Lloyd C. Trotman
, Nicole Mosberger
, Maarten Fornerod
, Robert P. Stidwill
, Urs F. Greber^*

^*Corresponding author for this work

University of Zurich
Netherlands Cancer Institute

Research output: Contribution to journal › Article › Academic › peer-review

277 Citations (Scopus)

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.

Original language	English
Pages (from-to)	1092-1100
Number of pages	9
Journal	Nature Cell Biology
Volume	3
Issue number	12
DOIs	https://doi.org/10.1038/ncb1201-1092
Publication status	Published - 1 Dec 2001
Externally published	Yes

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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.",

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AU - Stidwill, Robert P.

AU - Greber, Urs F.

PY - 2001/12/1

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AB - 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.

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EP - 1100

JO - Nature Cell Biology

JF - Nature Cell Biology

IS - 12

ER -

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

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