Yu Z, Kleifeld O, Lande-Atir A, Bsoul M, Kleiman M, Krutauz D, Book A, Vierstra RD, Hofmann K, Reis N, Glickman MH, Pick E

Subunit composition and architectural structure of the 26S proteasome lid is strictly conserved between all eukaryotes. This eight-subunit complex bears high similarity to the eukaryotic translation initiation factor 3 (eIF3) and to the COP9 signalosome (CSN) which together define the PCI troika. In some unicellular eukaryotes, the latter two complexes ...

Read More

lack key subunits, questioning the conservation of their structural design. Here we demonstrate that in S. cerevisiae, Rpn5 plays dual roles by stabilizing proteasome and CSN structures independently. Proteasome and CSN complexes are easily dissected, with Rpn5 the only subunit in common. Together with Rpn5, we identified a total of six bona fide subunits at roughly stoichiometric ratios in isolated affinity-purified CSN. Moreover, the copy of Rpn5 associated with the CSN is required for enzymatic hydrolysis of Rub1/Nedd8 conjugated to cullins. We propose that multitasking by a single subunit; Rpn5 in this case, allows it to function in different complexes simultaneously. These observations demonstrate that functional substitution of subunits by paralogs is feasible, implying that the canonical composition of the three PCI complexes in S. cerevisiae is more robust than hitherto appreciated.

Date: Feb. 02, 2011

View in: Pubmed Google Scholar

113028