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J. Virol. doi:10.1128/JVI.02532-07
Copyright (c) 2008, American Society for Microbiology and/or the Listed Authors/Institutions. All Rights Reserved.

E4Orf6-E1B-55k-dependent degradation of de novo-generated AAV5 Rep52 and capsid proteins employs a cullin 5-containing E3 ligase complex

Department of Molecular Microbiology and Immunology, University of Missouri-Columbia, School of Medicine, Life Sciences Center, Columbia, MO 65211

^* To whom correspondence should be addressed. Email: pinteld{at}missouri.edu.

	Abstract

Degradation of de novo-generated AAV5 Rep52 and capsid proteins is part of the limited target specificity displayed by Ad5 E4Orf6-E1B-55k as part of a cullin 5-containing E3 ligase complex. Both rep and capsid proteins can be found in the ligase complex, and their presence is dependent on interaction between E4Orf6 and elongins B and C. Degradation of AAV5 proteins can be inhibited by a dominant-negative ubiquitin that prevents chain elongation or by siRNA directed against cullin 5.