期刊
BIOCHEMICAL SOCIETY TRANSACTIONS
卷 32, 期 -, 页码 731-732出版社
PORTLAND PRESS LTD
DOI: 10.1042/BST0320731
关键词
affinity chromatography; DNA replication; EBNA1; immortalization; p53; tandem affinity purification (TAP) tagging
USP7 (also called HAUSP) is a de-ubiquitinating enzyme recently identified as a key regulator of the p53-mdm2 pathway, which stabilizes both p53 and mdm2. We have discovered that the Epstein-Barr nuclear antigen 1 protein of Epstein-Barr virus binds with high affinity to USP7 and disrupts the USP7-p53 interaction. The results have important implications for the role of Epstein-Barr nuclear antigen 1 in the cellular immortalization that is typical of an Epstein-Barr virus latent infection.
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