The carboxy terminus of the herpesvirus saimiri ORF 57 gene contains domains that are required for transactivation and transrepression
| Autor: | Michael A. Calderwood, Kersten T. Hall, Delyth J. Goodwin, Adrian Whitehouse, Alex F. Markham, Mathew S. Giles |
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| Rok vydání: | 2000 |
| Předmět: |
Gene Expression Regulation
Viral Transcriptional Activation Genes Viral Protein Conformation viruses DNA Mutational Analysis Molecular Sequence Data Quantitative Structure-Activity Relationship Biology Homology (biology) Herpesvirus 2 Saimiriine Transactivation Viral Proteins Protein structure Virology Animals Amino Acid Sequence Psychological repression Peptide sequence Cells Cultured Transrepression Zinc finger Genetics Base Sequence Reverse Transcriptase Polymerase Chain Reaction Zinc Fingers Repressor Proteins Mutagenesis Site-Directed Trans-Activators Aotidae Protein Processing Post-Translational Nuclear localization sequence |
| Zdroj: | The Journal of general virology. 81(Pt 9) |
| ISSN: | 0022-1317 |
| Popis: | Herpesvirus saimiri (HVS) ORF 57 is homologous to genes identified in all classes of herpesviruses. We have previously shown that ORF 57 encodes a multifunctional protein, responsible for both transactivation and repression of viral gene expression at a post-transcriptional level. This suggests that the ORF 57 protein shares some functional similarities with the herpes simplex virus IE63/ICP27 and Epstein–Barr virus Mta proteins. However, little is known about the functional domains responsible for the properties of ORF 57 due to the limited homology shared between these proteins. In this report, we have identified the functional domains responsible for transactivation and repression by the ORF 57 protein. We demonstrate that the carboxy terminus is required for ORF 57 transactivation, repression and an intense SC-35 nuclear spotting. This region contains two highly conserved motifs amongst its homologues, a zinc finger-like motif and a highly hydrophobic domain. We further show that the hydrophobic domain is required for transactivation and is also involved in nuclear localization of the ORF 57 protein, whereas the zinc finger-like domain is required for transactivation, repression and the intense SC-35 nuclear spotting. |
| Databáze: | OpenAIRE |
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