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The central unit within the 19S regulatory particle of the proteasome

The 26S proteasome is a multisubunit enzyme composed of a cylindrical catalytic core (20S) and a regulatory particle (19S) that together perform the essential degradation of cellular proteins tagged by ubiquitin. To date, however, substrate trajectory within the complex remains elusive. Here we desc...

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Detalles Bibliográficos
Autores principales: Rosenzweig, Rina, Osmulski, Pawel A, Gaczynska, Maria, Glickman, Michael H
Formato: Texto
Lenguaje:English
Publicado: 2008
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2481239/
https://www.ncbi.nlm.nih.gov/pubmed/18511945
http://dx.doi.org/10.1038/nsmb.1427
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author Rosenzweig, Rina
Osmulski, Pawel A
Gaczynska, Maria
Glickman, Michael H
author_facet Rosenzweig, Rina
Osmulski, Pawel A
Gaczynska, Maria
Glickman, Michael H
author_sort Rosenzweig, Rina
collection PubMed
description The 26S proteasome is a multisubunit enzyme composed of a cylindrical catalytic core (20S) and a regulatory particle (19S) that together perform the essential degradation of cellular proteins tagged by ubiquitin. To date, however, substrate trajectory within the complex remains elusive. Here we describe a previously unknown functional unit within the 19S, comprising two subunits, Rpn1 and Rpn2. These toroids physically link the site of substrate recruitment with the site of proteolysis. Rpn2 interfaces with the 20S, whereas Rpn1 sits atop Rpn2, serving as a docking site for a substrate-recruitment factor. The 19S ATPases encircle the Rpn1-Rpn2 stack, covering the remainder of the 20S surface. Both Rpn1-Rpn2 and the ATPases are required for substrate translocation and gating of the proteolytic channel. Similar pairing of units is found in unfoldases and nuclear transporters, exposing common features of these protein nanomachines.
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spelling pubmed-24812392008-12-01 The central unit within the 19S regulatory particle of the proteasome Rosenzweig, Rina Osmulski, Pawel A Gaczynska, Maria Glickman, Michael H Nat Struct Mol Biol Article The 26S proteasome is a multisubunit enzyme composed of a cylindrical catalytic core (20S) and a regulatory particle (19S) that together perform the essential degradation of cellular proteins tagged by ubiquitin. To date, however, substrate trajectory within the complex remains elusive. Here we describe a previously unknown functional unit within the 19S, comprising two subunits, Rpn1 and Rpn2. These toroids physically link the site of substrate recruitment with the site of proteolysis. Rpn2 interfaces with the 20S, whereas Rpn1 sits atop Rpn2, serving as a docking site for a substrate-recruitment factor. The 19S ATPases encircle the Rpn1-Rpn2 stack, covering the remainder of the 20S surface. Both Rpn1-Rpn2 and the ATPases are required for substrate translocation and gating of the proteolytic channel. Similar pairing of units is found in unfoldases and nuclear transporters, exposing common features of these protein nanomachines. 2008-05-30 2008-06 /pmc/articles/PMC2481239/ /pubmed/18511945 http://dx.doi.org/10.1038/nsmb.1427 Text en http://www.nature.com/authors/editorial_policies/license.html#terms Users may view, print, copy, and download text and data-mine the content in such documents, for the purposes of academic research, subject always to the full Conditions of use:http://www.nature.com/authors/editorial_policies/license.html#terms
spellingShingle Article
Rosenzweig, Rina
Osmulski, Pawel A
Gaczynska, Maria
Glickman, Michael H
The central unit within the 19S regulatory particle of the proteasome
title The central unit within the 19S regulatory particle of the proteasome
title_full The central unit within the 19S regulatory particle of the proteasome
title_fullStr The central unit within the 19S regulatory particle of the proteasome
title_full_unstemmed The central unit within the 19S regulatory particle of the proteasome
title_short The central unit within the 19S regulatory particle of the proteasome
title_sort central unit within the 19s regulatory particle of the proteasome
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2481239/
https://www.ncbi.nlm.nih.gov/pubmed/18511945
http://dx.doi.org/10.1038/nsmb.1427
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