Functional interactions between the Epstein-Barr virus BZLF1 protein and the promyelocytic leukemia protein

Autor: Brandy L. Bowling, Amy L. Adamson
Rok vydání: 2005
Předmět:
Transcriptional Activation
Cancer Research
viruses
Blotting
Western
Gene Expression
Plasma protein binding
Promyelocytic Leukemia Protein
medicine.disease_cause
Chromosomes
Transactivation
Promyelocytic leukemia protein
Viral Proteins
Interferon
Genes
Reporter
hemic and lymphatic diseases
Virology
MHC class I
medicine
Humans
Luciferases
Cellular localization
Tumor Necrosis Factor alpha-Induced Protein 3
Microscopy
Confocal
biology
Tumor Suppressor Proteins
Histocompatibility Antigens Class I
Intracellular Signaling Peptides and Proteins
virus diseases
Nuclear Proteins
Proteins
Epstein–Barr virus
BZLF1
Cell biology
Artificial Gene Fusion
Neoplasm Proteins
DNA-Binding Proteins
Infectious Diseases
Microscopy
Fluorescence
biology.protein
Cancer research
Trans-Activators
medicine.drug
HeLa Cells
Protein Binding
Transcription Factors
Zdroj: Virus research. 117(2)
ISSN: 0168-1702
Popis: The Epstein-Barr virus immediate-early protein BZLF1 (Z) has been shown to alter the cellular localization of the promyelocytic leukemia (PML) protein. PML has important implications for growth control, apoptosis, anti-viral effects and many more processes. Here we further examined the relationship between PML and the Epstein-Barr virus Z protein. We examined the effect of Z expression on PML protein levels, and the effect of increased PML protein levels on Z-mediated dispersion of PML bodies. We found that increased levels of PML protein, such as through interferon treatment, were able to suppress Z-mediated PML body dispersion. We also studied the consequences of PML dispersion by Z, by examining p21 transactivation, A20 transactivation, and MHC Class I presentation levels in Z-expressing cells. We found that, while Z-mediated dispersion of PML did not affect MHC Class I presentation, it did alter p21 and A20 expression. In addition, we found that increased levels of PML were able to prevent Z protein binding to mitotic chromosomes. Our work implies that the balance of PML and Z levels in cells may affect how each protein functions.
Databáze: OpenAIRE
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