E4Orf6-E1B-55k-dependent degradation of de novo-generated adeno-associated virus type 5 Rep52 and capsid proteins employs a cullin 5-containing E3 ligase complex.
Degradation of de novo-generated adeno-associated virus type 5 (AAV5) Rep52 and capsid proteins is part of the limited target specificity displayed by adenovirus type 5 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 small interfering RNA directed against cullin 5.
Nayak
Ramnath
R
Department of Molecular Microbiology and Immunology, University of Missouri-Columbia, School of Medicine, Life Sciences Center, Columbia, Missouri 65211, USA.
Farris
K David
KD
Pintel
David J
DJ
D002460:Cell Line; D044842:Cullin Proteins / Q000378:metabolism*; D000229:Dependovirus / Q000502:physiology*; D006801:Humans; D044767:Ubiquitin-Protein Ligases / Q000378:metabolism*; D014764:Viral Proteins / Q000378:metabolism*
C496871:CUL5 protein, human; D044842:Cullin Proteins; D014764:Viral Proteins; D044767:Ubiquitin-Protein Ligases