The BioGRID | PUBLICATION VIEW

	FEBS Lett. May (2007); 581(13):2567-73
Rpn13p and Rpn14p are involved in the recognition of ubiquitinated Gcn4p by the 26S proteasome-
Seong KM, Baek JH, Yu MH, Kim J
Laboratory of Biochemistry, School of Life Sciences and Biotechnology, Korea University, Seoul 136-701, Republic of Korea-
Abstract: The 26S proteasome, composed of the 20S core and 19S regulatory complexes, is important for the turnover of polyubiquitinated proteins- Each subunit of the complex plays a special role in proteolytic function, including substrate recruitment, deubiquitination, and structural contribution- To assess the function of some non-essential subunits in the 26S proteasome, we isolated the 26S proteasome from deletion strains of RPN13 and RPN14 using TAP affinity purification- The stability of Gcn4p and the accumulation of ubiquitinated Gcn4p were significantly increased, but the affinity in the recognition of proteasome was decreased- In addition, the subcomplexes of the isolated 26S proteasomes from deletion mutants were less stable than that of the wild type- Taken together, our findings indicate that Rpn13p and Rpn14p are involved in the efficient recognition of 26S proteasome for the proteolysis of ubiquitinated Gcn4p-
[PUBMED: 17499717]