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Journal of Virology, December 2007, p. 12881-12888, Vol. 81, No. 23
0022-538X/07/$08.00+0 doi:10.1128/JVI.00913-07
Copyright © 2007, American Society for Microbiology. All Rights Reserved.

Dongyuan Ma,1,
Jiangli Dong,1
Jingchen Jin,2
Daofeng Li,1
Changwang Deng,1 and
Tao Wang1*
State Key Laboratory for Agro-biotechnology, China Agricultural University, Beijing 100094, People's Republic of China,1 Henan Agricultural University, Zhengzhou 450002, People's Republic of China2
Received 28 April 2007/ Accepted 16 September 2007
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 ahead of print on 26 September 2007.
Dongyuan Ma and Yongsheng Jin contributed equally to this work.
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