This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Parkinson, J.
Right arrow Articles by Everett, R. D.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Parkinson, J.
Right arrow Articles by Everett, R. D.

 Previous Article  |  Next Article 

Journal of Virology, June 2001, p. 5357-5362, Vol. 75, No. 11
0022-538X/01/$04.00+0   DOI: 10.1128/JVI.75.11.5357-5362.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

Alphaherpesvirus Proteins Related to Herpes Simplex Virus Type 1 ICP0 Induce the Formation of Colocalizing, Conjugated Ubiquitin

Jane Parkinson* and Roger D. Everett

MRC Virology Unit, Glasgow G11 5JR, Scotland, United Kingdom

Received 1 November 2000/Accepted 2 March 2001

Herpes simplex virus type 1 immediate early protein ICP0 influences virus infection by inducing the degradation of specific cellular proteins via a mechanism requiring its RING finger and the ubiquitin-proteasome pathway. Many RING finger proteins, by virtue of their RING finger domain, interact with E2 ubiquitin-conjugating enzymes and act as a component of an E3 ubiquitin ligase. We have recently shown that ICP0 induces the accumulation of colocalizing, conjugated ubiquitin, suggesting that ICP0 can act as or contribute to an E3 ubiquitin ligase. In this report we demonstrate that the ICP0-related RING finger proteins encoded by other alphaherpesviruses also induce colocalizing, conjugated ubiquitin, thereby suggesting that they act by similar biochemical mechanisms.

* Corresponding author. Mailing address: MRC Virology Unit, Church St., Glasgow G11 5JR, Scotland, United Kingdom. Phone: (44)141 330 4017. Fax: (44)141 337 2236. E-mail: j.parkinson{at}vir.gla.ac.uk.

Journal of Virology, June 2001, p. 5357-5362, Vol. 75, No. 11
0022-538X/01/$04.00+0   DOI: 10.1128/JVI.75.11.5357-5362.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.


This article has been cited by other articles:

  • Wilkinson, D. E., Weller, S. K. (2006). Herpes simplex virus type I disrupts the ATR-dependent DNA-damage response during lytic infection. J. Cell Sci. 119: 2695-2703 [Abstract] [Full Text]  
  • Pomeranz, L. E., Reynolds, A. E., Hengartner, C. J. (2005). Molecular Biology of Pseudorabies Virus: Impact on Neurovirology and Veterinary Medicine. Microbiol. Mol. Biol. Rev. 69: 462-500 [Abstract] [Full Text]  
  • Wang, Z., Chua, H. K., Gusti, A. A. R. A., He, F., Fenner, B., Manopo, I., Wang, H., Kwang, J. (2005). RING-H2 Protein WSSV249 from White Spot Syndrome Virus Sequesters a Shrimp Ubiquitin-Conjugating Enzyme, PvUbc, for Viral Pathogenesis. J. Virol. 79: 8764-8772 [Abstract] [Full Text]  
  • Zhang, Y., Zhou, J., Jones, C. (2005). Identification of functional domains within the bICP0 protein encoded by bovine herpesvirus 1. J. Gen. Virol. 86: 879-886 [Abstract] [Full Text]  
  • Hagglund, R., Roizman, B. (2004). Role of ICP0 in the Strategy of Conquest of the Host Cell by Herpes Simplex Virus 1. J. Virol. 78: 2169-2178 [Full Text]  
  • Hagglund, R., Roizman, B. (2003). Herpes Simplex Virus 1 Mutant in Which the ICP0 HUL-1 E3 Ubiquitin Ligase Site Is Disrupted Stabilizes cdc34 but Degrades D-Type Cyclins and Exhibits Diminished Neurotoxicity. J. Virol. 77: 13194-13202 [Abstract] [Full Text]  
  • Hagglund, R., Van Sant, C., Lopez, P., Roizman, B. (2002). Herpes simplex virus 1-infected cell protein 0 contains two E3 ubiquitin ligase sites specific for different E2 ubiquitin-conjugating enzymes. Proc. Natl. Acad. Sci. USA 99: 631-636 [Abstract] [Full Text]  
  • Boutell, C., Sadis, S., Everett, R. D. (2002). Herpes Simplex Virus Type 1 Immediate-Early Protein ICP0 and Its Isolated RING Finger Domain Act as Ubiquitin E3 Ligases In Vitro. J. Virol. 76: 841-850 [Abstract] [Full Text]  
  • Van Sant, C., Hagglund, R., Lopez, P., Roizman, B. (2001). The infected cell protein 0 of herpes simplex virus 1 dynamically interacts with proteasomes, binds and activates the cdc34 E2 ubiquitin-conjugating enzyme, and possesses in vitro E3 ubiquitin ligase activity. Proc. Natl. Acad. Sci. USA 10.1073/pnas.161283098v1 [Abstract] [Full Text]  
  • Van Sant, C., Hagglund, R., Lopez, P., Roizman, B. (2001). The infected cell protein 0 of herpes simplex virus 1 dynamically interacts with proteasomes, binds and activates the cdc34 E2 ubiquitin-conjugating enzyme, and possesses in vitro E3 ubiquitin ligase activity. Proc. Natl. Acad. Sci. USA 98: 8815-8820 [Abstract] [Full Text]  


Copyright © 2009 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»