Abstract
Nucleocytoplasmic shuttling and interaction with the cellular mRNA export factor UAP56 are prerequisites for the mRNA export activity of human cytomegalovirus (HCMV) pUL69. Although the murine cytomegalovirus homolog pM69 shuttles, it fails to export mRNAs due to its inability to recruit UAP56. However, chimeric proteins comprising pM69 fused to N-terminal pUL69 fragments, including its UAP56 interaction motif, acquire mRNA export activity. Importantly, growth curves of recombinant HCMVs illustrate that such a chimeric protein, but not pM69, substitutes for pUL69 during HCMV infection.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Animals
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Biological Transport
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Cytomegalovirus / genetics
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Cytomegalovirus / physiology
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DEAD-box RNA Helicases / metabolism*
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Humans
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Mice
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Muromegalovirus / genetics*
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Muromegalovirus / physiology
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RNA, Messenger / metabolism
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RNA, Viral / metabolism
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Recombinant Proteins / genetics
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Recombinant Proteins / metabolism
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Trans-Activators / genetics*
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Trans-Activators / metabolism*
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Virus Replication*
Substances
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RNA, Messenger
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RNA, Viral
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Recombinant Proteins
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Trans-Activators
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pUL69 protein, Human herpesvirus 5
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DDX39B protein, human
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DEAD-box RNA Helicases