ATP hydrolysis-dependent disassembly of the 26S proteasome is part of the catalytic cycle Journal Article
| Authors: | Babbitt, S. E.; Kiss, A.; Deffenbaugh, A. E.; Chang, Y. H.; Bailly, E.; Erdjument-Bromage, H.; Tempst, P.; Buranda, T.; Sklar, L. A.; Baumler, J.; Gogol, E.; Skowyra, D. |
| Article Title: | ATP hydrolysis-dependent disassembly of the 26S proteasome is part of the catalytic cycle |
| Abstract: | ATP hydrolysis is required for degradation of polyubiquitinated proteins by the 26S proteasome but is thought to play no role in proteasomal stability during the catalytic cycle. In contrast to this view, we report that ATP hydrolysis triggers rapid dissociation of the 19S regulatory particles from immunopurified 26S complexes in a manner coincident with release of the bulk of proteasome-interacting proteins. Strikingly, this mechanism leads to quantitative disassembly of the 19S into subcomplexes and free Rpn10, the polyubiquitin binding subunit. Biochemical reconstitution with purified Sic1, a prototype substrate of the Cdc34/SCF ubiquitin ligase, suggests that substrate degradation is essential for triggering the ATP hydrolysis-dependent dissociation and disassembly of the 19S and that this mechanism leads to release of degradation products. This is the first demonstration that a controlled dissociation of the 19S regulatory particles from the 26S proteasome is part of the mechanism of protein degradation. Copyright ©2005 by Elsevier Inc. |
| Keywords: | controlled study; unclassified drug; nonhuman; ubiquitin; microscopy, electron; complex formation; proteasome; proteasome endopeptidase complex; ubiquitin protein ligase; enzyme degradation; protein assembly; enzyme substrate; saccharomyces cerevisiae; nucleotide sequence; carrier proteins; protein secretion; yeast; saccharomyces cerevisiae proteins; catalysis; adenosine triphosphate; protein subunits; polyubiquitin; adenosine triphosphatases; hydrolysis; enzyme purification; dissociation; fungal protein; enzyme mechanism; enzyme active site; protein hydrolysis; endopeptidases; ubiquitin-protein ligase complexes; proteasome interacting protein; ribophorin 10 |
| Journal Title: | Cell |
| Volume: | 121 |
| Issue: | 4 |
| ISSN: | 0092-8674 |
| Publisher: | Cell Press |
| Date Published: | 2005-05-20 |
| Start Page: | 553 |
| End Page: | 565 |
| Language: | English |
| DOI: | 10.1016/j.cell.2005.03.028 |
| PUBMED: | 15907469 |
| PROVIDER: | scopus |
| DOI/URL: | |
| Notes: | --- - "Cited By (since 1996): 73" - "Export Date: 24 October 2012" - "CODEN: CELLB" - "Molecular Sequence Numbers: GENBANK: SC0355, YE1350;" - "Source: Scopus" |
