Latency-associated Nuclear Antigen of Kaposi's Sarcoma-associated Herpesvirus Functionally Interacts with Heterochromatin Protein 1
| Autor: | Chunghun Lim, Taegun Seo, Daeyoup Lee, Joonho Choe, Changtaek Choi |
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| Rok vydání: | 2003 |
| Předmět: |
Transcription
Genetic Chromosomal Proteins Non-Histone Heterochromatin viruses Biology Transfection medicine.disease_cause Biochemistry Cell Line Genes Reporter medicine Transcriptional regulation Humans Nuclear protein Kaposi's sarcoma-associated herpesvirus Promoter Regions Genetic Antigens Viral Molecular Biology Cell Nucleus Genetics DNA replication Nuclear Proteins virus diseases Cell Biology biochemical phenomena metabolism and nutrition Position-effect variegation Precipitin Tests Protein Structure Tertiary Cell biology Cell nucleus medicine.anatomical_structure Microscopy Fluorescence Chromobox Protein Homolog 5 Herpesvirus 8 Human Mutation Heterochromatin protein 1 Gene Deletion Plasmids Protein Binding Subcellular Fractions |
| Zdroj: | ResearcherID |
| ISSN: | 0021-9258 |
| Popis: | Latency-associated nuclear antigen (LANA) of Kaposi's sarcoma-associated herpesvirus plays an important role in maintenance of the viral genome during latent infection. LANA additionally participates in the transcriptional regulation of several viral and cellular promoters. When tethered to constitutively active promoters, the protein exhibits transcriptional repressor activity. In this report, we further characterized cell type-, promoter-, and domain-specific transcriptional repression by LANA. We additionally speculated on the mechanism underlying transcriptional repression by the C terminus of the protein. Subnuclear localization patterns and association with heterochromatin suggested a possible link between LANA and heterochromatin protein 1, a representative heterochromatin-associated protein. In vivo and in vitro binding and immunofluorescence assays revealed that LANA associates with heterochromatin protein 1 in an isotype-specific manner. Furthermore, biochemical fractionation and transient replication assays supported the possibility that this interaction contributes to transcriptional repression, targeting to subnuclear structures, and latent DNA replication activity of LANA. |
| Databáze: | OpenAIRE |
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