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Journal of Virology, January 2003, p. 923-930, Vol. 77, No. 2
0022-538X/03/$08.00+0     DOI: 10.1128/JVI.77.2.923-930.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.

Ubiquitin Ligase Activities of Bombyx mori Nucleopolyhedrovirus RING Finger Proteins

Noriko Imai,1 Noriyuki Matsuda,2,3 Keiji Tanaka,3 Akihiko Nakano,2 Shogo Matsumoto,1 and WonKyung Kang1*

Laboratory of Molecular Entomology and Baculovirology,1 Laboratory of Molecular Membrane Biology, RIKEN, Wako 351-0198,2 Tokyo Metropolitan Institute of Medical Science, Tokyo 113-8613, Japan3

Received 6 September 2002/ Accepted 21 October 2002

The genome of Bombyx mori nucleopolyhedrovirus (BmNPV) is predicted to contain six RING finger proteins: IAP1, ORF35, IAP2, CG30, IE2, and PE38. Several other members of the RING finger family have recently been shown to have the ubiquitin-ligase (E3) activity. We thus examined whether BmNPV RING finger proteins have the E3 activity. In vitro ubiquitination assay with the rabbit reticulocyte lysates and BmNPV RING finger proteins fused with maltose-binding protein (MBP) showed that four of them (IAP2, IE2, PE38, and CG30) were polyubiquitinated in the presence of zinc ion. Furthermore, MBP-IAP2, MBP-IE2, and MBP-PE38 were able to reconstitute ubiquitination activity in cooperation with the Ubc4/5 subfamily of ubiquitin-conjugating enzymes. Mutational analysis also showed that ubiquitination activity of MBP-IAP2, MBP-IE2, and MBP-PE38 were dependent on their RING finger motif. Therefore, these results suggest that IAP2, IE2, and PE38 may function as E3 enzymes during BmNPV infection.

* Corresponding author. Mailing address: Laboratory of Molecular Entomology and Baculovirology, RIKEN, 2-1 Hirosawa, Wako 351-0198, Japan. Phone: 81-48-467-9584. Fax: 81-48-462-4678. E-mail: wkkang{at}postman.riken.go.jp.

Journal of Virology, January 2003, p. 923-930, Vol. 77, No. 2
0022-538X/03/$08.00+0     DOI: 10.1128/JVI.77.2.923-930.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.





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