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Open AccessArticle

In-depth Analysis of the Lid Subunits Assembly Mechanism in Mammals

Laboratory of Protein Metabolism, Graduate School of Pharmaceutical Sciences, The University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo 113-0033, Japan
Author to whom correspondence should be addressed.
Biomolecules 2019, 9(6), 213;
Received: 25 April 2019 / Revised: 21 May 2019 / Accepted: 29 May 2019 / Published: 31 May 2019
(This article belongs to the Special Issue The Broader Cellular Impact of Proteasome-CSN-eIf3 (PCI) Complexes)
The 26S proteasome is a key player in the degradation of ubiquitinated proteins, comprising a 20S core particle (CP) and a 19S regulatory particle (RP). The RP is further divided into base and lid subcomplexes, which are assembled independently from each other. We have previously demonstrated the assembly pathway of the CP and the base by observing assembly intermediates resulting from knockdowns of each proteasome subunit and the assembly chaperones. In this study, we examine the assembly pathway of the mammalian lid, which remains to be elucidated. We show that the lid assembly pathway is conserved between humans and yeast. The final step is the incorporation of Rpn12 into the assembly intermediate consisting of two modular complexes, Rpn3-7-15 and Rpn5-6-8-9-11, in both humans and yeast. Furthermore, we dissect the assembly pathways of the two modular complexes by the knockdown of each lid subunit. View Full-Text
Keywords: 26S proteasome; 19S regulatory particle; lid subcomplex; Rpn proteins; assembly 26S proteasome; 19S regulatory particle; lid subcomplex; Rpn proteins; assembly
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MDPI and ACS Style

Bai, M.; Zhao, X.; Sahara, K.; Ohte, Y.; Hirano, Y.; Kaneko, T.; Yashiroda, H.; Murata, S. In-depth Analysis of the Lid Subunits Assembly Mechanism in Mammals. Biomolecules 2019, 9, 213.

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