Source:http://linkedlifedata.com/resource/pubmed/id/11831723
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
2002-2-7
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pubmed:abstractText |
Both varicella-zoster virus open reading frame 4 (ORF4) protein and its herpes simplex virus type 1 homolog ICP27 have highly acidic amino-terminal regions and cysteine-rich carboxy-terminal regions. To investigate the functional domains of these proteins, mutants were constructed and their transregulatory functions were tested in transient expression assays using two reporter plasmids, pTK-CAT-SV40A and pTK-CAT-synA, containing the same promoter sequences but different mRNA processing signals. ORF4 transactivates both pTK-CAT-SV40A and pTK-CAT-synA, while ICP27 transrepresses pTK-CAT-SV40A and transactivates pTK-CAT-synA. Deletion of the ORF4 amino-terminal region abolished most of the transactivating activity for pTK-CAT-synA but retained most of the transactivating activity for pTK-CAT-SV40A. Construction of chimeric ORF4-ICP27 molecules indicated that the ORF4 amino-terminal region was able to replace the corresponding region of ICP27 which is required for both transrepression of pTK-CAT-SV40A and transactivation of pTK-CAT-synA. Similarly, the ICP27 amino-terminal region was able to partially replace the corresponding region of ORF4 which is required for transactivation of pTK-CAT-synA Thus, while ORF4 and ICP27 have different properties in transient expression assays, the amino-terminal regions of ORF4 and ICP27 are functionally homologous to each other and are important in regulating gene expression.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/ICP27 protein, human herpesvirus 1,
http://linkedlifedata.com/resource/pubmed/chemical/Immediate-Early Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/ORF4 protein, Human herpesvirus 3,
http://linkedlifedata.com/resource/pubmed/chemical/Trans-Activators,
http://linkedlifedata.com/resource/pubmed/chemical/Viral Proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
0042-6822
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
1
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pubmed:volume |
208
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
376-82
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:11831723-Amino Acid Sequence,
pubmed-meshheading:11831723-Gene Expression Regulation, Viral,
pubmed-meshheading:11831723-Herpesvirus 1, Human,
pubmed-meshheading:11831723-Herpesvirus 3, Human,
pubmed-meshheading:11831723-Humans,
pubmed-meshheading:11831723-Immediate-Early Proteins,
pubmed-meshheading:11831723-Molecular Sequence Data,
pubmed-meshheading:11831723-Trans-Activators,
pubmed-meshheading:11831723-Transcriptional Activation,
pubmed-meshheading:11831723-Viral Proteins,
pubmed-meshheading:11831723-Virus Replication
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pubmed:year |
1995
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pubmed:articleTitle |
The acidic amino-terminal region of varicella-zoster virus open reading frame 4 protein is required for transactivation and can functionally replace the corresponding region of herpes simplex virus ICP27.
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pubmed:affiliation |
Laboratory of Clinical Investigation, National Institute of Allergy and Infectious Diseases, Bethesda, Maryland 20892, USA.
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pubmed:publicationType |
Journal Article
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