Serine-173 of the Epstein-Barr virus ZEBRA protein is required for DNA binding and is a target for casein kinase II phosphorylation
| Autor: | Naomi Taylor, J L Kolman, George Miller, Daniel R. Marshak |
|---|---|
| Rok vydání: | 1993 |
| Předmět: |
Transcriptional Activation
Herpesvirus 4 Human animal structures Transcription Genetic genetic structures Proto-Oncogene Proteins c-jun Recombinant Fusion Proteins Molecular Sequence Data Mutant Protein Serine-Threonine Kinases Biology Polymerase Chain Reaction Viral Proteins chemistry.chemical_compound Transcription (biology) Escherichia coli Serine Humans Point Mutation Amino Acid Sequence Cloning Molecular Phosphorylation Binding site Casein Kinase II Promoter Regions Genetic DNA Primers B-Lymphocytes Alanine Binding Sites Multidisciplinary Base Sequence DNA-binding domain Molecular biology DNA-Binding Proteins nervous system chemistry Lytic cycle Mutagenesis Site-Directed Trans-Activators behavior and behavior mechanisms Casein kinase 2 Proto-Oncogene Proteins c-fos psychological phenomena and processes DNA Research Article |
| Zdroj: | Proceedings of the National Academy of Sciences. 90:10115-10119 |
| ISSN: | 1091-6490 0027-8424 |
| DOI: | 10.1073/pnas.90.21.10115 |
| Popis: | An Epstein-Barr virus-encoded protein, ZEBRA, mediates the switch from latency to the viral lytic life cycle. ZEBRA's domain structure and DNA binding specificity resemble that of cellular transcriptional activators such as c-Fos/c-Jun. We show that ZEBRA, like c-Jun, is phosphorylated by casein kinase II (CKII). The principal site of phosphorylation is serine-173 (S173), five amino acids upstream of the basic DNA recognition domain. CKII phosphorylation abrogated ZEBRA's capacity to bind its target DNA sequences. S173 is a functional component of ZEBRA's DNA binding domain, since mutation of S173 to alanine (S173A) reduced DNA binding in vitro to 10% of wild-type levels. Transcriptional activation of a native viral promoter in vivo by mutant S173A was also reduced markedly. Reversible phosphorylation of S173 is likely to be an important means of regulating ZEBRA's activity in vivo. |
| Databáze: | OpenAIRE |
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