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ABSTRACT:
SUBMITTER: Nakayama S
PROVIDER: S-EPMC3004297 | biostudies-literature | 2010 Dec
REPOSITORIES: biostudies-literature
Nakayama Sanae S Murata Takayuki T Yasui Yoshihiro Y Murayama Kazutaka K Isomura Hiroki H Kanda Teru T Tsurumi Tatsuya T
Journal of virology 20101006 24
The Epstein-Barr virus BMRF1 DNA polymerase processivity factor, which is essential for viral genome replication, exists mainly as a C-shaped head-to-head homodimer but partly forms a ring-shaped tetramer through tail-to-tail association. Based on its molecular structure, several BMRF1 mutant viruses were constructed to examine their influence on viral replication. The R256E virus, which has a severely impaired capacity for DNA binding and polymerase processivity, failed to form replication comp ...[more]