TY - JOUR
T1 - Tetrameric ring formation of Epstein-Barr virus polymerase processivity factor is crucial for viral replication
AU - Nakayama, Sanae
AU - Murata, Takayuki
AU - Yasui, Yoshihiro
AU - Murayama, Kazutaka
AU - Isomura, Hiroki
AU - Kanda, Teru
AU - Tsurumi, Tatsuya
PY - 2010/12
Y1 - 2010/12
N2 - 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 compartments, resulting in interference of viral replication, while the C95E mutation, which impairs head-to-head contact in vitro, unexpectedly hardly affected the viral replication. Also, surprisingly, replication of the C206E virus, which is expected to have impairment of tail-to-tail contact, was severely restricted, although the mutant protein possesses the same in vitro biochemical activities as the wild type. Since the tail-to-tail contact surface is smaller than that of the head-to-head contact area, its contribution to ring formation might be essential for viral replication.
AB - 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 compartments, resulting in interference of viral replication, while the C95E mutation, which impairs head-to-head contact in vitro, unexpectedly hardly affected the viral replication. Also, surprisingly, replication of the C206E virus, which is expected to have impairment of tail-to-tail contact, was severely restricted, although the mutant protein possesses the same in vitro biochemical activities as the wild type. Since the tail-to-tail contact surface is smaller than that of the head-to-head contact area, its contribution to ring formation might be essential for viral replication.
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U2 - 10.1128/JVI.01394-10
DO - 10.1128/JVI.01394-10
M3 - Article
C2 - 20926567
AN - SCOPUS:78649392657
SN - 0022-538X
VL - 84
SP - 12589
EP - 12598
JO - Journal of Virology
JF - Journal of Virology
IS - 24
ER -