ACTA VETERINARIA ET ZOOTECHNICA SINICA ›› 2015, Vol. 46 ›› Issue (12): 2127-2134.doi: 10.11843/j.issn.0366-6964.2015.12.002

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Poxvirus Encode Proteins with E3 Ubiquitin Ligase Function

CHEN Yi-xia*,SHAO Zhong-wei,LI Gui-hua,WANG Cong   

  1. (College of Life Science and Engineering,Northwest University for Nationalities,Lanzhou 730124,China)
  • Received:2015-05-05 Online:2015-12-23 Published:2015-12-23

Abstract:

Ubiquitylation is a covalent post-translational modification that regulates protein stability and is involved in many biological functions.Many poxviruses have evolved multiple mechanisms to perturb the cell ubiquitin system and manipulate it to their own benefit.Such as the poxvirus family encode ubiquitin ligases with intrinsic activity,including the membrane-associated RING-CH(MARCH) domain,p28/Really Interesting New Gene(RING) finger,ankyrin-repeat/F-box and Broad-complex,Tramtrack and Bric-a-Brac(BTB)/Kelch subgroups of the E3 Ub ligase superfamily.Here we describe and discuss the proteins with E3 ubiquitin ligase function encoded by poxvirus.

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