期刊
JOURNAL OF MOLECULAR BIOLOGY
卷 391, 期 4, 页码 717-728出版社
ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD
DOI: 10.1016/j.jmb.2009.06.034
关键词
herpesvirus; replication; exonuclease; ribonuclease; crystal structure
资金
- European Commission [QLG2_CT_200200988]
- French government
- Dutch Cancer Foundation [RUL 2005-3259]
- Royal Dutch Academy of Sciences
- Netherlands Scientific Organization [NWO Vidi 917.76.330]
Epstein-Barr virus, a double-stranded DNA (dsDNA) virus, is a major human pathogen from the herpesvirus family. The nuclease is one of the lytic cycle proteins required for successful viral replication. In addition to the previously described endonuclease and exonuclease activities on single-stranded DNA and dsDNA substrates, we observed an RNase activity for Epstein-Barr virus nuclease in the presence of Mn2+ giving a possible explanation for its role in host mRNA degradation. Its crystal structure shows a catalytic core of the D-(D/E)XK nuclease superfamily closely related to the exonuclease from bacteriophage lambda with a bridge across the active-site canyon. This bridge may reduce endonuclease activity, ensure processivity or play a role in strand separation of dsDNA substrates. As the DNA strand that is subject to cleavage is likely to make a sharp turn in front of the bridge, endonuclease activity on single-stranded DNA stretches appears to be possible, explaining the cleavage of circular substrates. (C) 2009 Elsevier Ltd. All rights reserved.
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