Unknown

Dataset Information

0

An atomic model AAA-ATPase/20S core particle sub-complex of the 26S proteasome.


ABSTRACT: The 26S proteasome is the most downstream element of the ubiquitin-proteasome pathway of protein degradation. It is composed of the 20S core particle (CP) and the 19S regulatory particle (RP). The RP consists of 6 AAA-ATPases and at least 13 non-ATPase subunits. Based on a cryo-EM map of the 26S proteasome, structures of homologs, and physical protein-protein interactions we derive an atomic model of the AAA-ATPase-CP sub-complex. The ATPase order in our model (Rpt1/Rpt2/Rpt6/Rpt3/Rpt4/Rpt5) is in excellent agreement with the recently identified base-precursor complexes formed during the assembly of the RP. Furthermore, the atomic CP-AAA-ATPase model suggests that the assembly chaperone Nas6 facilitates CP-RP association by enhancing the shape complementarity between Rpt3 and its binding CP alpha subunits partners.

SUBMITTER: Forster F 

PROVIDER: S-EPMC2771176 | biostudies-literature | 2009 Oct

REPOSITORIES: biostudies-literature

altmetric image

Publications

An atomic model AAA-ATPase/20S core particle sub-complex of the 26S proteasome.

Förster Friedrich F   Lasker Keren K   Beck Florian F   Nickell Stephan S   Sali Andrej A   Baumeister Wolfgang W  

Biochemical and biophysical research communications 20090803 2


The 26S proteasome is the most downstream element of the ubiquitin-proteasome pathway of protein degradation. It is composed of the 20S core particle (CP) and the 19S regulatory particle (RP). The RP consists of 6 AAA-ATPases and at least 13 non-ATPase subunits. Based on a cryo-EM map of the 26S proteasome, structures of homologs, and physical protein-protein interactions we derive an atomic model of the AAA-ATPase-CP sub-complex. The ATPase order in our model (Rpt1/Rpt2/Rpt6/Rpt3/Rpt4/Rpt5) is  ...[more]

Similar Datasets

| S-EPMC3992659 | biostudies-literature
| S-EPMC5893597 | biostudies-literature
| S-EPMC94466 | biostudies-literature
| S-EPMC4295373 | biostudies-literature
| S-EPMC2743420 | biostudies-literature
| S-EPMC5458511 | biostudies-literature
| S-EPMC8379623 | biostudies-literature
| S-EPMC9856285 | biostudies-literature
| S-EPMC3869383 | biostudies-literature