Structure of an endogenous yeast 26S proteasome reveals two major conformational states
The eukaryotic proteasome mediates degradation of polyubiquitinated proteins. Here we report the single-particle cryoelectron microscopy (cryo-EM) structures of the endogenous 26S proteasome from Saccharomyces cerevisiae at 4.6- to 6.3-Å resolution. The fine features of the cryo-EM maps allow modeli...
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| Published in | Proceedings of the National Academy of Sciences - PNAS Vol. 113; no. 10; pp. 2642 - 2647 |
|---|---|
| Main Authors | , , , , , , , , , , , , , , |
| Format | Journal Article |
| Language | English |
| Published |
United States
National Academy of Sciences
08.03.2016
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| Subjects | |
| Online Access | Get full text |
| ISSN | 0027-8424 1091-6490 1091-6490 |
| DOI | 10.1073/pnas.1601561113 |
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| Abstract | The eukaryotic proteasome mediates degradation of polyubiquitinated proteins. Here we report the single-particle cryoelectron microscopy (cryo-EM) structures of the endogenous 26S proteasome from Saccharomyces cerevisiae at 4.6- to 6.3-Å resolution. The fine features of the cryo-EM maps allow modeling of 18 subunits in the regulatory particle and 28 in the core particle. The proteasome exhibits two distinct conformational states, designated M1 and M2, which correspond to those reported previously for the proteasome purified in the presence of ATP-γS and ATP, respectively. These conformations also correspond to those of the proteasome in the presence and absence of exogenous substrate. Structure-guided biochemical analysis reveals enhanced deubiquitylating enzyme activity of Rpn11 upon assembly of the lid. Our structures serve as a molecular basis for mechanistic understanding of proteasome function. |
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| AbstractList | The eukaryotic proteasome mediates degradation of polyubiquitinated proteins. Here we report the single-particle cryoelectron microscopy (cryo-EM) structures of the endogenous 26S proteasome from Saccharomyces cerevisiae at 4.6- to 6.3-Å resolution. The fine features of the cryo-EM maps allow modeling of 18 subunits in the regulatory particle and 28 in the core particle. The proteasome exhibits two distinct conformational states, designated M1 and M2, which correspond to those reported previously for the proteasome purified in the presence of ATP-γS and ATP, respectively. These conformations also correspond to those of the proteasome in the presence and absence of exogenous substrate. Structure-guided biochemical analysis reveals enhanced deubiquitylating enzyme activity of Rpn11 upon assembly of the lid. Our structures serve as a molecular basis for mechanistic understanding of proteasome function.The eukaryotic proteasome mediates degradation of polyubiquitinated proteins. Here we report the single-particle cryoelectron microscopy (cryo-EM) structures of the endogenous 26S proteasome from Saccharomyces cerevisiae at 4.6- to 6.3-Å resolution. The fine features of the cryo-EM maps allow modeling of 18 subunits in the regulatory particle and 28 in the core particle. The proteasome exhibits two distinct conformational states, designated M1 and M2, which correspond to those reported previously for the proteasome purified in the presence of ATP-γS and ATP, respectively. These conformations also correspond to those of the proteasome in the presence and absence of exogenous substrate. Structure-guided biochemical analysis reveals enhanced deubiquitylating enzyme activity of Rpn11 upon assembly of the lid. Our structures serve as a molecular basis for mechanistic understanding of proteasome function. The eukaryotic proteasome mediates degradation of polyubiquitinated proteins. Here we report the single-particle cryoelectron microscopy (cryo-EM) structures of the endogenous 26S proteasome from Saccharomyces cerevisiae at 4.6- to 6.3-Å resolution. The fine features of the cryo-EM maps allow modeling of 18 subunits in the regulatory particle and 28 in the core particle. The proteasome exhibits two distinct conformational states, designated M1 and M2, which correspond to those reported previously for the proteasome purified in the presence of ATP-γS and ATP, respectively. These conformations also correspond to those of the proteasome in the presence and absence of exogenous substrate. Structure-guided biochemical analysis reveals enhanced deubiquitylating enzyme activity of Rpn11 upon assembly of the lid. Our structures serve as a molecular basis for mechanistic understanding of proteasome function. The eukaryotic proteasome mediates degradation of polyubiquitinated proteins. Here we report the single-particle cryoelectron microscopy (cryo-EM) structures of the endogenous 26S proteasome from Saccharomyces cerevisiae at 4.6- to 6.3-A resolution. The fine features of the cryo-EM maps allow modeling of 18 subunits in the regulatory particle and 28 in the core particle. The proteasome exhibits two distinct conformational states, designated M1 and M2, which correspond to those reported previously for the proteasome purified in the presence of ATP-γS and ATP, respectively. These conformations also correspond to those of the proteasome in the presence and absence of exogenous substrate. Structure-guided biochemical analysis reveals enhanced deubiquitylating enzyme activity of Rpn11 upon assembly of the lid. Our structures serve as a molecular basis for mechanistic understanding of proteasome function. The eukaryotic proteasome mediates degradation of polyubiquitinated proteins. Here we report the single-particle cryoelectron microscopy (cryo-EM) structures of the endogenous 26S proteasome from Saccharomyces cerevisiae at 4.6- to 6.3-A resolution. The fine features of the cryo-EM maps allow modeling of 18 subunits in the regulatory particle and 28 in the core particle. The proteasome exhibits two distinct conformational states, designated M1 and M2, which correspond to those reported previously for the proteasome purified in the presence of ATP- gamma S and ATP, respectively. These conformations also correspond to those of the proteasome in the presence and absence of exogenous substrate. Structure-guided biochemical analysis reveals enhanced deubiquitylating enzyme activity of Rpn11 upon assembly of the lid. Our structures serve as a molecular basis for mechanistic understanding of proteasome function. Mechanistic understanding of proteasome function requires elucidation of its three-dimensional structure. Previous investigations have revealed increasingly detailed information on the overall organization of the yeast 26S proteasome. In this study, we further improved the resolution of cryo-EM structures of endogenous proteasomes from Saccharomyces cerevisiae . These structures reveal two distinct conformational states, which appear to correspond to different states of ATP hydrolysis and substrate binding. This information may guide future functional analysis of the proteasome. The eukaryotic proteasome mediates degradation of polyubiquitinated proteins. Here we report the single-particle cryoelectron microscopy (cryo-EM) structures of the endogenous 26S proteasome from Saccharomyces cerevisiae at 4.6- to 6.3-Å resolution. The fine features of the cryo-EM maps allow modeling of 18 subunits in the regulatory particle and 28 in the core particle. The proteasome exhibits two distinct conformational states, designated M1 and M2, which correspond to those reported previously for the proteasome purified in the presence of ATP-γS and ATP, respectively. These conformations also correspond to those of the proteasome in the presence and absence of exogenous substrate. Structure-guided biochemical analysis reveals enhanced deubiquitylating enzyme activity of Rpn11 upon assembly of the lid. Our structures serve as a molecular basis for mechanistic understanding of proteasome function. Mechanistic understanding of proteasome function requires elucidation of its three-dimensional structure. Previous investigations have revealed increasingly detailed information on the overall organization of the yeast 26S proteasome. In this study, we further improved the resolution of cryo-EM structures of endogenous proteasomes from Saccharomyces cerevisiae. These structures reveal two distinct conformational states, which appear to correspond to different states of ATP hydrolysis and substrate binding. This information may guide future functional analysis of the proteasome. The eukaryotic proteasome mediates degradation of polyubiquitinated proteins. Here we report the single-particle cryoelectron microscopy (cryo-EM) structures of the endogenous 26S proteasome from Saccharomyces cerevisiae at 4.6- to 6.3-Å resolution. The fine features of the cryo-EM maps allow modeling of 18 subunits in the regulatory particle and 28 in the core particle. The proteasome exhibits two distinct conformational states, designated M1 and M2, which correspond to those reported previously for the proteasome purified in the presence of ATP-γS and ATP, respectively. These conformations also correspond to those of the proteasome in the presence and absence of exogenous substrate. Structure-guided biochemical analysis reveals enhanced deubiquitylating enzyme activity of Rpn11 upon assembly of the lid. Our structures serve as a molecular basis for mechanistic understanding of proteasome function. SignificanceMechanistic understanding of proteasome function requires elucidation of its three-dimensional structure. Previous investigations have revealed increasingly detailed information on the overall organization of the yeast 26S proteasome. In this study, we further improved the resolution of cryo-EM structures of endogenous proteasomes from Saccharomyces cerevisiae. These structures reveal two distinct conformational states, which appear to correspond to different states of ATP hydrolysis and substrate binding. This information may guide future functional analysis of the proteasome. The eukaryotic proteasome mediates degradation of polyubiquitinated proteins. Here we report the single-particle cryoelectron microscopy (cryo-EM) structures of the endogenous 26S proteasome from Saccharomyces cerevisiae at 4.6- to 6.3-Å resolution. The fine features of the cryo-EM maps allow modeling of 18 subunits in the regulatory particle and 28 in the core particle. The proteasome exhibits two distinct conformational states, designated M1 and M2, which correspond to those reported previously for the proteasome purified in the presence of ATP-γS and ATP, respectively. These conformations also correspond to those of the proteasome in the presence and absence of exogenous substrate. Structure-guided biochemical analysis reveals enhanced deubiquitylating enzyme activity of Rpn11 upon assembly of the lid. Our structures serve as a molecular basis for mechanistic understanding of proteasome function. |
| Author | Finley, Daniel J. Huang, Xiuliang Mei, Ziqing Wang, Jiawei Wang, Yiwei Luan, Bai Yan, Chuangye 王丰 施一公 Wang, Feng Wu, Jianping 栾白 Xue, Xiaobin Shi, Yigong 黄修良 |
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| Copyright | Volumes 1–89 and 106–113, copyright as a collective work only; author(s) retains copyright to individual articles Copyright National Academy of Sciences Mar 8, 2016 |
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| Notes | SourceType-Scholarly Journals-1 ObjectType-Feature-1 content type line 14 ObjectType-Article-1 ObjectType-Feature-2 content type line 23 1B.L. and X.H. contributed equally to this work. Contributed by Yigong Shi, February 4, 2016 (sent for review January 5, 2016; reviewed by Aaron Ciechanover and Huilin Li) Author contributions: B.L., X.H., Y.S., and F.W. designed research; B.L., X.H., J. Wu, Z.M., Y.W., X.X., and F.W. performed research; B.L., X.H., J. Wu, C.Y., J. Wang, D.J.F., Y.S., and F.W. analyzed data; and B.L., X.H., J. Wu, D.J.F., Y.S., and F.W. wrote the paper. Reviewers: A.C., Technion–Israel Institute of Technology; and H.L., Stony Brook University. |
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| Snippet | The eukaryotic proteasome mediates degradation of polyubiquitinated proteins. Here we report the single-particle cryoelectron microscopy (cryo-EM) structures... SignificanceMechanistic understanding of proteasome function requires elucidation of its three-dimensional structure. Previous investigations have revealed... Mechanistic understanding of proteasome function requires elucidation of its three-dimensional structure. Previous investigations have revealed increasingly... |
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| SubjectTerms | Adenosine triphosphatase ATP Biochemical analysis Biochemistry Biological Sciences Cryoelectron Microscopy - methods Crystallography, X-Ray Enzymatic activity Eukaryotes Models, Molecular Proteasome Endopeptidase Complex - chemistry Proteasome Endopeptidase Complex - metabolism Proteasome Endopeptidase Complex - ultrastructure Protein Conformation Proteins Proteolysis Saccharomyces cerevisiae Saccharomyces cerevisiae - enzymology Saccharomyces cerevisiae Proteins - chemistry Saccharomyces cerevisiae Proteins - metabolism Saccharomyces cerevisiae Proteins - ultrastructure Substrate Specificity Yeast Yeasts |
| Title | Structure of an endogenous yeast 26S proteasome reveals two major conformational states |
| URI | https://www.jstor.org/stable/26468602 https://www.pnas.org/doi/10.1073/pnas.1601561113 https://www.ncbi.nlm.nih.gov/pubmed/26929360 https://www.proquest.com/docview/1774332936 https://www.proquest.com/docview/1772146674 https://www.proquest.com/docview/1785232751 https://pubmed.ncbi.nlm.nih.gov/PMC4790998 https://www.pnas.org/content/pnas/113/10/2642.full.pdf |
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