1. HC-Pro Protein of Potato Virus Y Can Interact with Three Arabidopsis 20S Proteasome Subunits In Planta
- Author
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Yong-Sheng Jin, Changwang Deng, Dongyuan Ma, Jingchen Jin, Jiangli Dong, Daofeng Li, and Tao Wang
- Subjects
Proteasome Endopeptidase Complex ,Protein subunit ,Potyvirus ,Immunology ,Mutant ,Arabidopsis ,Mutation, Missense ,Plasma protein binding ,Microbiology ,Viral Proteins ,Two-Hybrid System Techniques ,Virology ,Protein Interaction Mapping ,Plant Proteins ,Sequence Deletion ,chemistry.chemical_classification ,biology ,biology.organism_classification ,Yeast ,Virus-Cell Interactions ,N-terminus ,Cysteine Endopeptidases ,Enzyme ,Amino Acid Substitution ,Potato virus Y ,Biochemistry ,chemistry ,Insect Science ,Protein Binding - Abstract
The multifunctional protein helper component proteinase (HC-Pro) is thought to interfere with the activity of the 20S proteasome; however, no sites of interaction have been identified for either protein. Here, we first show that the Potato virus Y (PVY) HC-Pro protein can interact with three Arabidopsis 20S proteasome subunits (PAA, PBB, and PBE), using a yeast two-hybrid system and the bimolecular fluorescence complement assay. In addition, yeast two-hybrid analysis of the interaction between several mutant subunits of the 20S proteasome and PVY HC-Pro confirmed that residues 81 to 140 of PAA, 1 to 80 of PBB, and 160 to 274 of PBE are necessary for binding PAA, PBB, and PBE to PVY HC-Pro, respectively. Deletion mutant analysis of PVY HC-Pro showed that the N terminus (residues 1 to 97) is necessary for its interaction with three Arabidopsis 20S proteasome subunits. The ability of HC-Pro to interact and interfere with the activity of the 20S proteasome may help explain the molecular basis of its multifunctional character.
- Published
- 2007