scholarly journals Human origin recognition complex binds to the region of the latent origin of DNA replication of Epstein-Barr virus

2001 ◽  
Vol 20 (16) ◽  
pp. 4588-4602 ◽  
Author(s):  
A. Schepers
Keyword(s):  
Dna Replication ◽  
Epstein Barr Virus ◽  
Origin Recognition Complex ◽  
Human Origin ◽  
Barr Virus ◽  
Origin Of Dna Replication ◽  
Epstein Barr ◽  
Origin Recognition

scholarly journals Regulation of Epstein-Barr Virus OriP Replication by Poly(ADP-Ribose) Polymerase 1

2010 ◽  
Vol 84 (10) ◽  
pp. 4988-4997 ◽  
Author(s):  
Italo Tempera ◽  
Zhong Deng ◽  
Constandache Atanasiu ◽  
Chi-Ju Chen ◽  
Maria D'Erme ◽  
...  
Keyword(s):  
Dna Replication ◽  
Dna Binding ◽  
Epstein Barr Virus ◽  
Origin Recognition Complex ◽  
Structural Changes ◽  
Replication Initiation ◽  
Barr Virus ◽  
Ds Element ◽  
Epstein Barr

ABSTRACT Poly(ADP-ribose) polymerase (PARP) is an abundant, chromatin-associated, NAD-dependent enzyme that functions in multiple chromosomal processes, including DNA replication and chromatin remodeling. The Epstein-Barr virus (EBV) origin of plasmid replication (OriP) is a dynamic genetic element that confers stable episome maintenance, DNA replication initiation, and chromatin organization functions. OriP function depends on the EBV-encoded origin binding protein EBNA1. We have previously shown that EBNA1 is subject to negative regulation by poly(ADP-ribosyl)ation (PARylation). We now show that PARP1 physically associates with OriP in latently EBV-infected B cells. Short hairpin RNA depletion of PARP1 enhances OriP replication activity and increases EBNA1, origin recognition complex 2 (ORC2), and minichromosome maintenance complex (MCM) association with OriP. Pharmacological inhibitors of PARP1 enhance OriP plasmid maintenance and increase EBNA1, ORC2, and MCM3 occupancy at OriP. PARylation in vitro inhibits ORC2 recruitment and remodels telomere repeat factor (TRF) binding at the dyad symmetry (DS) element of OriP. Purified PARP1 can ribosylate EBNA1 at multiple sites throughout its amino terminus but not in the carboxy-terminal DNA binding domain. We also show that EBNA1 linking regions (LR1 and LR2) can bind directly to oligomers of PAR. We propose that PARP1-dependent PARylation of EBNA1 and adjacently bound TRF2 induces structural changes at the DS element that reduce EBNA1 DNA binding affinity and functional recruitment of ORC.

scholarly journals Activation oforiLyt,the Lytic Origin of DNA Replication of Epstein–Barr Virus, by BZLF1

Virology ◽  
1996 ◽  
Vol 220 (2) ◽  
pp. 367-376 ◽  
Author(s):  
ALOYS SCHEPERS ◽  
DAGMAR PICH ◽  
WOLFGANG HAMMERSCHMIDT
Keyword(s):  
Dna Replication ◽  
Epstein Barr Virus ◽  
Barr Virus ◽  
Origin Of Dna Replication ◽  
Epstein Barr

scholarly journals Role for G-Quadruplex RNA Binding by Epstein-Barr Virus Nuclear Antigen 1 in DNA Replication and Metaphase Chromosome Attachment

2009 ◽  
Vol 83 (20) ◽  
pp. 10336-10346 ◽  
Author(s):  
Julie Norseen ◽  
F. Brad Johnson ◽  
Paul M. Lieberman
Keyword(s):  
Dna Replication ◽  
Epstein Barr Virus ◽  
Origin Recognition Complex ◽  
Rna Binding ◽  
Binding Capacity ◽  
Nuclear Antigen ◽  
Metaphase Chromosomes ◽  
Barr Virus ◽  
G Quadruplex ◽  
Epstein Barr

ABSTRACT Latent infection by Epstein-Barr virus (EBV) requires both replication and maintenance of the viral genome. EBV nuclear antigen 1 (EBNA1) is a virus-encoded protein that is critical for the replication and maintenance of the genome during latency in proliferating cells. We have previously demonstrated that EBNA1 recruits the cellular origin recognition complex (ORC) through an RNA-dependent interaction with EBNA1 linking region 1 (LR1) and LR2. We now show that LR1 and LR2 bind to G-rich RNA that is predicted to form G-quadruplex structures. Several chemically distinct G-quadruplex-interacting drugs disrupted the interaction between EBNA1 and ORC. The G-quadruplex-interacting compound BRACO-19 inhibited EBNA1-dependent stimulation of viral DNA replication and preferentially blocked proliferation of EBV-positive cells relative to EBV-negative cell lines. BRACO-19 treatment also disrupted the ability of EBNA1 to tether to metaphase chromosomes, suggesting that maintenance function is also mediated through G-quadruplex recognition. These findings suggest that the EBNA1 replication and maintenance function uses a common G-quadruplex binding capacity of LR1 and LR2, which may be targetable by small-molecule inhibitors.

De Novo DNA Methylation at Nonrandom Founder Sites 5' from an Unmethylated Minimal Origin of DNA Replication in Latent Epstein-Barr Virus Genomes

2000 ◽  
Vol 381 (2) ◽  
Author(s):  
Daniel Salamon ◽  
Maria Takacs ◽  
Sanna Myöhänen ◽  
Zoltan Marcsek ◽  
György Berencsi ◽  
...  
Keyword(s):  
Dna Methylation ◽  
Dna Replication ◽  
Epstein Barr Virus ◽  
De Novo ◽  
Barr Virus ◽  
Origin Of Dna Replication ◽  
Epstein Barr ◽  
Virus Genomes
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