Human RPA (hSSB) interacts with EBNA1, the latent origin binding protein of Epstein-Barr virus.
AUTOR(ES)
Zhang, D
RESUMO
RPA is the replicative single-strand DNA (ssDNA) binding protein of eukaryotic chromosomes. This report shows that human RPA interacts with EBNA1, the latent origin binding protein of Epstein-Barr virus (EBV). RPA binds to EBNA1 both in solution, and when EBNA1 is bound to the EBV origin. RPA is a heterotrimer, and the main contact with EBNA1 is formed through the 70 kDa subunit of RPA, the subunit which binds to ssDNA. We propose that this interaction between RPA and EBNA1 is an early step in activation of the latent origin of EBV.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=147273Documentos Relacionados
- EBNA1 distorts oriP, the Epstein-Barr virus latent replication origin.
- Epstein-Barr nuclear antigen 1 mediates a DNA loop within the latent replication origin of Epstein-Barr virus.
- Functional Analyses of the EBNA1 Origin DNA Binding Protein of Epstein-Barr Virus
- Cooperative assembly of EBNA1 on the Epstein-Barr virus latent origin of replication.
- Constitutive binding of EBNA1 protein to the Epstein-Barr virus replication origin, oriP, with distortion of DNA structure during latent infection.
