Linked Life Data

11831723

Source:http://linkedlifedata.com/resource/pubmed/id/11831723

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pubmed-article:11831723pubmed:abstractTextBoth 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.lld:pubmed
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pubmed-article:11831723pubmed:pagination376-82lld:pubmed
pubmed-article:11831723pubmed:dateRevised2008-11-21lld:pubmed
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pubmed-article:11831723pubmed:articleTitleThe 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.lld:pubmed
pubmed-article:11831723pubmed:affiliationLaboratory of Clinical Investigation, National Institute of Allergy and Infectious Diseases, Bethesda, Maryland 20892, USA.lld:pubmed
pubmed-article:11831723pubmed:publicationTypeJournal Articlelld:pubmed
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