The Activation Domain of Herpesvirus Saimiri R Protein Interacts with the TATA-Binding Protein
| Autor: | Alex J. Stevenson, Adrian Whitehouse, Paul C. Gibson, Delyth J. Goodwin, Kersten T. Hall, Alex F. Markham |
|---|---|
| Rok vydání: | 1999 |
| Předmět: |
Transcriptional Activation
viruses DNA Mutational Analysis Molecular Sequence Data Immunology Response Elements Microbiology DNA-binding protein Immediate early protein Cell Line Herpesvirus 2 Saimiriine Immediate-Early Proteins Viral Proteins Transactivation Virology Animals Amino Acid Sequence Promoter Regions Genetic Peptide sequence Binding Sites General transcription factor biology TATA-Box Binding Protein Molecular biology Virus-Cell Interactions DNA-Binding Proteins Open reading frame Insect Science Trans-Activators biology.protein Aotidae Rabbits TATA-binding protein Transcription Factors |
| Zdroj: | Journal of Virology. 73:9756-9763 |
| ISSN: | 1098-5514 0022-538X |
| DOI: | 10.1128/jvi.73.12.9756-9763.1999 |
| Popis: | The herpesvirus saimiri open reading frame (ORF) 50 produces two transcripts. The first is spliced, contains a single intron, and is detected at early times during the productive cycle, whereas the second is expressed later and is produced from a promoter within the second exon. Analysis of their gene products has shown that they function as sequence specific transactivators. In this report, we demonstrate that the carboxy terminus of ORF 50b contains an activation domain which is essential for transactivation. This domain contains positionally conserved hydrophobic residues found in a number of activation domains, including the herpes simplex virus VP16 and the Epstein-Barr virus R proteins. Mutational analysis of this domain demonstrates that these conserved hydrophobic residues are essential for ORF 50 transactivation capability. Furthermore, this domain is required for the interaction between the ORF 50 proteins and the basal transcription factor TATA-binding protein. |
| Databáze: | OpenAIRE |
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