Cryo-EM structures and dynamics of substrate-engaged human 26S proteasome
The proteasome is an ATP-dependent, 2.5-megadalton molecular machine that is responsible for selective protein degradation in eukaryotic cells. Here we present cryo-electron microscopy structures of the substrate-engaged human proteasome in seven conformational states at 2.8–3.6 Å resolution, captur...
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| Published in | Nature (London) Vol. 565; no. 7737; pp. 49 - 55 |
|---|---|
| Main Authors | , , , , , , , , , |
| Format | Journal Article |
| Language | English |
| Published |
London
Nature Publishing Group UK
01.01.2019
Nature Publishing Group |
| Subjects | |
| Online Access | Get full text |
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| Abstract | The proteasome is an ATP-dependent, 2.5-megadalton molecular machine that is responsible for selective protein degradation in eukaryotic cells. Here we present cryo-electron microscopy structures of the substrate-engaged human proteasome in seven conformational states at 2.8–3.6 Å resolution, captured during breakdown of a polyubiquitylated protein. These structures illuminate a spatiotemporal continuum of dynamic substrate–proteasome interactions from ubiquitin recognition to substrate translocation, during which ATP hydrolysis sequentially navigates through all six ATPases. There are three principal modes of coordinated hydrolysis, featuring hydrolytic events in two oppositely positioned ATPases, in two adjacent ATPases and in one ATPase at a time. These hydrolytic modes regulate deubiquitylation, initiation of translocation and processive unfolding of substrates, respectively. Hydrolysis of ATP powers a hinge-like motion in each ATPase that regulates its substrate interaction. Synchronization of ATP binding, ADP release and ATP hydrolysis in three adjacent ATPases drives rigid-body rotations of substrate-bound ATPases that are propagated unidirectionally in the ATPase ring and unfold the substrate.
Cryo-electron microscopy structures and dynamics of a substrate-engaged human 26S proteasome reveal in atomic detail three principal modes of coordinated ATP hydrolysis that regulate different steps in the degradation of a ubiquitylated protein. |
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| AbstractList | The proteasome is an ATP-dependent, 2.5-megadalton molecular machine that is responsible for selective protein degradation in eukaryotic cells. Here we present cryo-electron microscopy structures of the substrate-engaged human proteasome in seven conformational states at 2.8-3.6 Å resolution, captured during breakdown of a polyubiquitylated protein. These structures illuminate a spatiotemporal continuum of dynamic substrate-proteasome interactions from ubiquitin recognition to substrate translocation, during which ATP hydrolysis sequentially navigates through all six ATPases. There are three principal modes of coordinated hydrolysis, featuring hydrolytic events in two oppositely positioned ATPases, in two adjacent ATPases and in one ATPase at a time. These hydrolytic modes regulate deubiquitylation, initiation of translocation and processive unfolding of substrates, respectively. Hydrolysis of ATP powers a hinge-like motion in each ATPase that regulates its substrate interaction. Synchronization of ATP binding, ADP release and ATP hydrolysis in three adjacent ATPases drives rigid-body rotations of substrate-bound ATPases that are propagated unidirectionally in the ATPase ring and unfold the substrate. The proteasome is an ATP-dependent, 2.5-megadalton molecular machine that is responsible for selective protein degradation in eukaryotic cells. Here we present cryo-electron microscopy structures of the substrate-engaged human proteasome in seven conformational states at 2.8-3.6 Å resolution, captured during breakdown of a polyubiquitylated protein. These structures illuminate a spatiotemporal continuum of dynamic substrate-proteasome interactions from ubiquitin recognition to substrate translocation, during which ATP hydrolysis sequentially navigates through all six ATPases. There are three principal modes of coordinated hydrolysis, featuring hydrolytic events in two oppositely positioned ATPases, in two adjacent ATPases and in one ATPase at a time. These hydrolytic modes regulate deubiquitylation, initiation of translocation and processive unfolding of substrates, respectively. Hydrolysis of ATP powers a hinge-like motion in each ATPase that regulates its substrate interaction. Synchronization of ATP binding, ADP release and ATP hydrolysis in three adjacent ATPases drives rigid-body rotations of substrate-bound ATPases that are propagated unidirectionally in the ATPase ring and unfold the substrate.The proteasome is an ATP-dependent, 2.5-megadalton molecular machine that is responsible for selective protein degradation in eukaryotic cells. Here we present cryo-electron microscopy structures of the substrate-engaged human proteasome in seven conformational states at 2.8-3.6 Å resolution, captured during breakdown of a polyubiquitylated protein. These structures illuminate a spatiotemporal continuum of dynamic substrate-proteasome interactions from ubiquitin recognition to substrate translocation, during which ATP hydrolysis sequentially navigates through all six ATPases. There are three principal modes of coordinated hydrolysis, featuring hydrolytic events in two oppositely positioned ATPases, in two adjacent ATPases and in one ATPase at a time. These hydrolytic modes regulate deubiquitylation, initiation of translocation and processive unfolding of substrates, respectively. Hydrolysis of ATP powers a hinge-like motion in each ATPase that regulates its substrate interaction. Synchronization of ATP binding, ADP release and ATP hydrolysis in three adjacent ATPases drives rigid-body rotations of substrate-bound ATPases that are propagated unidirectionally in the ATPase ring and unfold the substrate. The proteasome is an ATP-dependent, 2.5-megadalton molecular machine that is responsible for selective protein degradation in eukaryotic cells. Here we present cryo-electron microscopy structures of the substrate-engaged human proteasome in seven conformational states at 2.8-3.6 Å resolution, captured during breakdown of a polyubiquitylated protein. These structures illuminate a spatiotemporal continuum of dynamic substrate-proteasome interactions from ubiquitin recognition to substrate translocation, during which ATP hydrolysis sequentially navigates through all six ATPases. There are three principal modes of coordinated hydrolysis, featuring hydrolytic events in two oppositely positioned ATPases, in two adjacent ATPases and in one ATPase at a time. These hydrolytic modes regulate deubiquitylation, initiation of translocation and processive unfolding of substrates, respectively. Hydrolysis of ATP powers a hinge-like motion in each ATPase that regulates its substrate interaction. Synchronization of ATP binding, ADP release and ATP hydrolysis in three adjacent ATPases drives rigid-body rotations of substrate-bound ATPases that are propagated unidirectionally in the ATPase ring and unfold the substrate.Cryo-electron microscopy structures and dynamics of a substrate-engaged human 26S proteasome reveal in atomic detail three principal modes of coordinated ATP hydrolysis that regulate different steps in the degradation of a ubiquitylated protein. The proteasome is an ATP-dependent, 2.5-megadalton molecular machine that is responsible for selective protein degradation in eukaryotic cells. Here we present cryo-electron microscopy structures of the substrate-engaged human proteasome in seven conformational states at 2.8–3.6 Å resolution, captured during breakdown of a polyubiquitylated protein. These structures illuminate a spatiotemporal continuum of dynamic substrate–proteasome interactions from ubiquitin recognition to substrate translocation, during which ATP hydrolysis sequentially navigates through all six ATPases. There are three principal modes of coordinated hydrolysis, featuring hydrolytic events in two oppositely positioned ATPases, in two adjacent ATPases and in one ATPase at a time. These hydrolytic modes regulate deubiquitylation, initiation of translocation and processive unfolding of substrates, respectively. Hydrolysis of ATP powers a hinge-like motion in each ATPase that regulates its substrate interaction. Synchronization of ATP binding, ADP release and ATP hydrolysis in three adjacent ATPases drives rigid-body rotations of substrate-bound ATPases that are propagated unidirectionally in the ATPase ring and unfold the substrate. Cryo-electron microscopy structures and dynamics of a substrate-engaged human 26S proteasome reveal in atomic detail three principal modes of coordinated ATP hydrolysis that regulate different steps in the degradation of a ubiquitylated protein. The proteasome is an ATP-dependent, 2.5-megadalton machine responsible for selective protein degradation in eukaryotic cells. Here we present cryo-EM structures of the substrate-engaged human proteasome in seven conformational states at 2.8-3.6 Å resolution, captured during breakdown of a polyubiquitylated protein. These structures visualize a continuum of dynamic substrate-proteasome interactions from ubiquitin recognition to substrate translocation, during which ATP hydrolysis sequentially navigates through all six ATPases. Three principal modes of coordinated hydrolysis are observed, featuring hydrolytic events in two oppositely positioned ATPases, in two adjacent ATPases, and in one ATPase at a time. These hydrolytic modes regulate deubiquitylation, translocation initiation and processive unfolding of substrates, respectively. ATP hydrolysis powers a hinge-like motion in each ATPase that regulates its substrate interaction. Synchronization of ATP binding, ADP release and ATP hydrolysis in three adjacent ATPases drives rigid-body rotations of substrate-bound ATPases that are propagated unidirectionally in the ATPase ring and unfold the substrate. The proteasome is an ATP-dependent, 2.5-megadalton molecular machine that is responsible for selective protein degradation in eukaryotic cells. Here we present cryo-electron microscopy structures of the substrate-engaged human proteasome in seven conformational states at 2.8-3.6 Å resolution, captured during breakdown of a polyubiquitylated protein. These structures illuminate a spatiotemporal continuum of dynamic substrate-proteasome interactions from ubiquitin recognition to substrate translocation, during which ATP hydrolysis sequentially navigates through all six ATPases. There are three principal modes of coordinated hydrolysis, featuring hydrolytic events in two oppositely positioned ATPases, in two adjacent ATPases and in one ATPase at a time. These hydrolytic modes regulate deubiquitylation, initiation of translocation and processive unfolding of substrates, respectively. Hydrolysis of ATP powers a hinge-like motion in each ATPase that regulates its substrate interaction. Synchronization of ATP binding, ADP release and ATP hydrolysis in three adjacent ATPases drives rigid-body rotations of substrate-bound ATPases that are propagated unidirectionally in the ATPase ring and unfold the substrate. |
| Audience | Academic |
| Author | Zhu, Yanan Lu, Ying Wu, Zhaolong Wang, Wei Li Stoilova-McPhie, Svetla Zhang, Shuwen Dong, Yuanchen Finley, Daniel Li, Xuemei Mao, Youdong |
| AuthorAffiliation | 8 Department of Cell Biology, Harvard Medical School, Boston, MA 02115, USA 7 Department of Systems Biology, Harvard Medical School, Boston, MA 02115, USA 6 Center for Nanoscale Systems, Harvard University, Cambridge, MA 02138, USA 3 Intel Parallel Computing Center for Structural Biology, Dana-Farber Cancer Institute, Boston, MA 02215, USA 1 State Key Laboratory for Artificial Microstructures and Mesoscopic Physics, School of Physics, Peking University, Beijing 100871, China 4 Department of Cancer Immunology and Virology, Dana-Farber Cancer Institute, Department of Microbiology and Immunobiology, Harvard Medical School, Boston, MA 02115, USA 5 Electron Microscopy Laboratory, School of Physics, Peking University, Beijing 100871, China 2 Center for Quantitative Biology, Peking University, Beijing 100871, China |
| AuthorAffiliation_xml | – name: 1 State Key Laboratory for Artificial Microstructures and Mesoscopic Physics, School of Physics, Peking University, Beijing 100871, China – name: 3 Intel Parallel Computing Center for Structural Biology, Dana-Farber Cancer Institute, Boston, MA 02215, USA – name: 7 Department of Systems Biology, Harvard Medical School, Boston, MA 02115, USA – name: 2 Center for Quantitative Biology, Peking University, Beijing 100871, China – name: 6 Center for Nanoscale Systems, Harvard University, Cambridge, MA 02138, USA – name: 4 Department of Cancer Immunology and Virology, Dana-Farber Cancer Institute, Department of Microbiology and Immunobiology, Harvard Medical School, Boston, MA 02115, USA – name: 5 Electron Microscopy Laboratory, School of Physics, Peking University, Beijing 100871, China – name: 8 Department of Cell Biology, Harvard Medical School, Boston, MA 02115, USA |
| Author_xml | – sequence: 1 givenname: Yuanchen surname: Dong fullname: Dong, Yuanchen organization: State Key Laboratory for Artificial Microstructures and Mesoscopic Physics, School of Physics, Peking University, Intel Parallel Computing Center for Structural Biology, Dana-Farber Cancer Institute, Department of Cancer Immunology and Virology, Dana-Farber Cancer Institute, Department of Microbiology and Immunobiology, Harvard Medical School – sequence: 2 givenname: Shuwen surname: Zhang fullname: Zhang, Shuwen organization: State Key Laboratory for Artificial Microstructures and Mesoscopic Physics, School of Physics, Peking University, Center for Quantitative Biology, Peking University – sequence: 3 givenname: Zhaolong surname: Wu fullname: Wu, Zhaolong organization: State Key Laboratory for Artificial Microstructures and Mesoscopic Physics, School of Physics, Peking University – sequence: 4 givenname: Xuemei surname: Li fullname: Li, Xuemei organization: Electron Microscopy Laboratory, School of Physics, Peking University – sequence: 5 givenname: Wei Li surname: Wang fullname: Wang, Wei Li organization: State Key Laboratory for Artificial Microstructures and Mesoscopic Physics, School of Physics, Peking University, Intel Parallel Computing Center for Structural Biology, Dana-Farber Cancer Institute, Department of Cancer Immunology and Virology, Dana-Farber Cancer Institute, Department of Microbiology and Immunobiology, Harvard Medical School – sequence: 6 givenname: Yanan surname: Zhu fullname: Zhu, Yanan organization: State Key Laboratory for Artificial Microstructures and Mesoscopic Physics, School of Physics, Peking University, Center for Quantitative Biology, Peking University – sequence: 7 givenname: Svetla surname: Stoilova-McPhie fullname: Stoilova-McPhie, Svetla organization: Center for Nanoscale Systems, Harvard University – sequence: 8 givenname: Ying surname: Lu fullname: Lu, Ying organization: Department of Systems Biology, Harvard Medical School – sequence: 9 givenname: Daniel surname: Finley fullname: Finley, Daniel organization: Department of Cell Biology, Harvard Medical School – sequence: 10 givenname: Youdong surname: Mao fullname: Mao, Youdong email: youdong_mao@dfci.harvard.edu organization: State Key Laboratory for Artificial Microstructures and Mesoscopic Physics, School of Physics, Peking University, Intel Parallel Computing Center for Structural Biology, Dana-Farber Cancer Institute, Department of Cancer Immunology and Virology, Dana-Farber Cancer Institute, Department of Microbiology and Immunobiology, Harvard Medical School, Center for Quantitative Biology, Peking University, Electron Microscopy Laboratory, School of Physics, Peking University |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/30479383$$D View this record in MEDLINE/PubMed |
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| Cites_doi | 10.1021/bi061994u 10.1016/j.cell.2011.02.005 10.1038/cr.2016.86 10.1016/j.cell.2009.09.034 10.1016/j.jsb.2015.11.003 10.1073/pnas.1120559109 10.1016/j.jsb.2005.07.007 10.1073/pnas.1305782110 10.1038/ncomms9520 10.1073/pnas.1614614113 10.1146/annurev-biochem-062917-011931 10.1016/S1097-2765(01)00308-2 10.1073/pnas.1601561113 10.1016/j.jsb.2005.03.010 10.1038/nmeth.4193 10.1016/S0076-6879(05)99014-9 10.1038/nsmb.1501 10.1073/pnas.1608050113 10.1016/j.celrep.2018.07.004 10.1038/nature10774 10.7554/eLife.13027 10.1073/pnas.1400546111 10.1074/jbc.M702846200 10.7554/eLife.18722 10.1126/science.1075898 10.1038/nmeth.2727 10.1038/nsmb.3273 10.1038/s41467-018-03785-w 10.1002/jcc.20084 10.1016/j.tibs.2015.10.009 10.1126/science.aan1052 10.1186/s12859-017-1757-y 10.1073/pnas.1621129114 10.1016/j.str.2011.12.015 10.1126/science.aad9421 10.7554/eLife.25754 10.1107/S0907444904019158 10.1073/pnas.1213333109 10.1016/j.molcel.2009.04.021 10.1016/j.molcel.2017.07.023 10.1126/science.aao0464 10.1126/sciadv.1701726 10.1038/nature04943 10.1016/j.molcel.2012.03.026 10.1016/j.cell.2004.06.014 10.1126/science.1250834 10.1016/j.jmb.2007.05.022 10.7554/eLife.31324 10.1038/s41467-018-04731-6 10.7554/eLife.24487 10.1038/nsmb.2771 10.1371/journal.pone.0182130 10.1016/j.molcel.2017.06.007 10.1016/j.cell.2009.08.043 10.1038/386463a0 10.1093/emboj/16.19.5847 10.1038/35040607 |
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| Notes | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 14 content type line 23 Author Contributions Y.D. purified proteins, conducted biochemical analysis and prepared samples for imaging. Y.D., S.Z., Z.W., X.L., W.L.W., Y.Z. and S.S.M. collected data. S.Z. and Z.W. processed the data and refined the maps. Y.D., S.Z., Y.L. and D.F. contributed to structural analysis and manuscript preparation. Y.M. conceived and supervised this study, devised the methods, performed atomic modeling, analyzed the structures and wrote the manuscript. |
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| References | Thomsen, Berger (CR46) 2009; 139 Snoberger, Brettrager, Smith (CR35) 2018; 9 Zhu (CR11) 2018; 9 Suloway (CR48) 2005; 151 Zhang (CR51) 2016; 193 Glynn, Martin, Nager, Baker, Sauer (CR36) 2009; 139 Kim, Snoberger, Schupp, Smith (CR37) 2015; 6 Lasker (CR15) 2012; 109 Eisele (CR12) 2018; 24 Livneh, Cohen-Kaplan, Cohen-Rosenzweig, Avni, Ciechanover (CR1) 2016; 26 Verma, McDonald, Yates, Deshaies (CR24) 2001; 8 Lander (CR16) 2012; 482 Wang (CR47) 2007; 46 Shi (CR6) 2016; 351 Dambacher, Worden, Herzik, Martin, Lander (CR32) 2016; 5 Verma (CR8) 2002; 298 Pettersen (CR58) 2004; 25 Śledź (CR21) 2013; 110 CR4 Gates (CR41) 2017; 357 Worden, Padovani, Martin (CR31) 2014; 21 Kimanius, Forsberg, Scheres, Lindahl (CR53) 2016; 5 He (CR34) 2012; 20 Adams (CR57) 2010 Zhang (CR28) 2009; 34 Smith, Fraga, Reis, Kafri, Goldberg (CR9) 2011; 144 Pathare (CR30) 2014; 111 Beck (CR20) 2012; 109 Monroe, Han, Shen, Sundquist, Hill (CR44) 2017; 6 Bard (CR3) 2018; 87 Wu (CR54) 2017; 12 Huang, Luan, Wu, Shi (CR18) 2016; 23 Chen (CR10) 2016; 113 Schweitzer (CR14) 2016; 113 CR59 Worden, Dong, Martin (CR29) 2017; 67 Horwitz (CR38) 2007; 282 Lu, Lee, King, Finley, Kirschner (CR25) 2015; 348 Enemark, Joshua-Tor (CR45) 2006; 442 Emsley, Cowtan (CR56) 2004; 60 Wehmer (CR13) 2017; 114 Mastronarde (CR49) 2005; 152 Krissinel, Henrick (CR60) 2007; 372 Saeki, Isono, Toh-E (CR23) 2005; 399 Puchades (CR39) 2017; 358 Ripstein, Huang, Augustyniak, Kay, Rubinstein (CR40) 2017; 6 Zheng (CR50) 2017; 14 CR27 CR26 Finley, Chen, Walters (CR2) 2016; 41 Han, Monroe, Sundquist, Shen, Hill (CR42) 2017; 6 CR22 Zhu, Ouyang, Mao (CR52) 2017; 18 Kucukelbir, Sigworth, Tagare (CR55) 2014; 11 Deville (CR43) 2017; 3 Verma, Oania, Graumann, Deshaies (CR7) 2004; 118 Luan (CR19) 2016; 113 Lu (CR5) 2017; 67 Zhang, Wigley (CR33) 2008; 15 da Fonseca, He, Morris (CR17) 2012; 46 Y Shi (736_CR6) 2016; 351 X Wang (736_CR47) 2007; 46 736_CR26 736_CR27 736_CR22 CM Dambacher (736_CR32) 2016; 5 SE Glynn (736_CR36) 2009; 139 F Beck (736_CR20) 2012; 109 GR Pathare (736_CR30) 2014; 111 SN Gates (736_CR41) 2017; 357 PD Adams (736_CR57) 2010 YC Kim (736_CR37) 2015; 6 DN Mastronarde (736_CR49) 2005; 152 R Verma (736_CR7) 2004; 118 I Livneh (736_CR1) 2016; 26 R Verma (736_CR24) 2001; 8 EJ Worden (736_CR31) 2014; 21 J Wu (736_CR54) 2017; 12 Y Lu (736_CR25) 2015; 348 N Monroe (736_CR44) 2017; 6 P Śledź (736_CR21) 2013; 110 C Puchades (736_CR39) 2017; 358 736_CR59 Y Saeki (736_CR23) 2005; 399 ZA Ripstein (736_CR40) 2017; 6 F Zhang (736_CR28) 2009; 34 J He (736_CR34) 2012; 20 A Snoberger (736_CR35) 2018; 9 A Kucukelbir (736_CR55) 2014; 11 Y Zhu (736_CR52) 2017; 18 S Chen (736_CR10) 2016; 113 Y Lu (736_CR5) 2017; 67 Y Zhu (736_CR11) 2018; 9 P Emsley (736_CR56) 2004; 60 MR Eisele (736_CR12) 2018; 24 JAM Bard (736_CR3) 2018; 87 D Finley (736_CR2) 2016; 41 DM Smith (736_CR9) 2011; 144 E Krissinel (736_CR60) 2007; 372 K Lasker (736_CR15) 2012; 109 D Kimanius (736_CR53) 2016; 5 EF Pettersen (736_CR58) 2004; 25 X Zhang (736_CR33) 2008; 15 ND Thomsen (736_CR46) 2009; 139 K Zhang (736_CR51) 2016; 193 A Schweitzer (736_CR14) 2016; 113 PC Fonseca da (736_CR17) 2012; 46 GC Lander (736_CR16) 2012; 482 C Deville (736_CR43) 2017; 3 C Suloway (736_CR48) 2005; 151 736_CR4 AA Horwitz (736_CR38) 2007; 282 X Huang (736_CR18) 2016; 23 SQ Zheng (736_CR50) 2017; 14 M Wehmer (736_CR13) 2017; 114 B Luan (736_CR19) 2016; 113 EJ Worden (736_CR29) 2017; 67 EJ Enemark (736_CR45) 2006; 442 R Verma (736_CR8) 2002; 298 H Han (736_CR42) 2017; 6 |
| References_xml | – volume: 46 start-page: 3553 year: 2007 end-page: 3565 ident: CR47 article-title: Mass spectrometric characterization of the affinity-purified human 26S proteasome complex publication-title: Biochemistry doi: 10.1021/bi061994u – ident: CR22 – volume: 144 start-page: 526 year: 2011 end-page: 538 ident: CR9 article-title: ATP binds to proteasomal ATPases in pairs with distinct functional effects, implying an ordered reaction cycle publication-title: Cell doi: 10.1016/j.cell.2011.02.005 – volume: 26 start-page: 869 year: 2016 end-page: 885 ident: CR1 article-title: The life cycle of the 26S proteasome: from birth, through regulation and function, and onto its death publication-title: Cell Res. doi: 10.1038/cr.2016.86 – volume: 139 start-page: 744 year: 2009 end-page: 756 ident: CR36 article-title: Structures of asymmetric ClpX hexamers reveal nucleotide-dependent motions in a AAA+ protein-unfolding machine publication-title: Cell doi: 10.1016/j.cell.2009.09.034 – ident: CR4 – volume: 193 start-page: 1 year: 2016 end-page: 12 ident: CR51 article-title: Gctf: Real-time CTF determination and correction publication-title: J. Struct. Biol. doi: 10.1016/j.jsb.2015.11.003 – volume: 109 start-page: 1380 year: 2012 end-page: 1387 ident: CR15 article-title: Molecular architecture of the 26S proteasome holocomplex determined by an integrative approach publication-title: Proc. Natl Acad. Sci. USA doi: 10.1073/pnas.1120559109 – volume: 152 start-page: 36 year: 2005 end-page: 51 ident: CR49 article-title: Automated electron microscope tomography using robust prediction of specimen movements publication-title: J. Struct. Biol. doi: 10.1016/j.jsb.2005.07.007 – volume: 110 start-page: 7264 year: 2013 end-page: 7269 ident: CR21 article-title: Structure of the 26S proteasome with ATP-γS bound provides insights into the mechanism of nucleotide-dependent substrate translocation publication-title: Proc. Natl Acad. Sci. USA doi: 10.1073/pnas.1305782110 – volume: 6 year: 2015 ident: CR37 article-title: ATP binding to neighbouring subunits and intersubunit allosteric coupling underlie proteasomal ATPase function publication-title: Nat. Commun. doi: 10.1038/ncomms9520 – volume: 113 start-page: 12991 year: 2016 end-page: 12996 ident: CR10 article-title: Structural basis for dynamic regulation of the human 26S proteasome publication-title: Proc. Natl Acad. Sci. USA doi: 10.1073/pnas.1614614113 – volume: 87 start-page: 697 year: 2018 end-page: 724 ident: CR3 article-title: Structure and function of the 26S proteasome publication-title: Annu. Rev. Biochem. doi: 10.1146/annurev-biochem-062917-011931 – volume: 8 start-page: 439 year: 2001 end-page: 448 ident: CR24 article-title: Selective degradation of ubiquitinated Sic1 by purified 26S proteasome yields active S phase cyclin-Cdk publication-title: Mol. Cell doi: 10.1016/S1097-2765(01)00308-2 – volume: 113 start-page: 2642 year: 2016 end-page: 2647 ident: CR19 article-title: Structure of an endogenous yeast 26S proteasome reveals two major conformational states publication-title: Proc. Natl Acad. Sci. USA doi: 10.1073/pnas.1601561113 – volume: 151 start-page: 41 year: 2005 end-page: 60 ident: CR48 article-title: Automated molecular microscopy: the new Leginon system publication-title: J. Struct. Biol. doi: 10.1016/j.jsb.2005.03.010 – volume: 14 start-page: 331 year: 2017 end-page: 332 ident: CR50 article-title: MotionCor2: anisotropic correction of beam-induced motion for improved cryo-electron microscopy publication-title: Nat. Methods doi: 10.1038/nmeth.4193 – volume: 399 start-page: 215 year: 2005 end-page: 227 ident: CR23 article-title: Preparation of ubiquitinated substrates by the PY motif-insertion method for monitoring 26S proteasome activity publication-title: Methods Enzymol. doi: 10.1016/S0076-6879(05)99014-9 – volume: 15 start-page: 1223 year: 2008 end-page: 1227 ident: CR33 article-title: The ‘glutamate switch’ provides a link between ATPase activity and ligand binding in AAA+ proteins publication-title: Nat. Struct. Mol. Biol. doi: 10.1038/nsmb.1501 – volume: 113 start-page: 7816 year: 2016 end-page: 7821 ident: CR14 article-title: Structure of the human 26S proteasome at a resolution of 3.9 Å publication-title: Proc. Natl Acad. Sci. USA doi: 10.1073/pnas.1608050113 – volume: 24 start-page: 1301 year: 2018 end-page: 1315 ident: CR12 article-title: Expanded coverage of the 26S proteasome conformational landscape reveals mechanisms of peptidase gating publication-title: Cell Rep. doi: 10.1016/j.celrep.2018.07.004 – volume: 482 start-page: 186 year: 2012 end-page: 191 ident: CR16 article-title: Complete subunit architecture of the proteasome regulatory particle publication-title: Nature doi: 10.1038/nature10774 – volume: 5 start-page: e13027 year: 2016 ident: CR32 article-title: Atomic structure of the 26S proteasome lid reveals the mechanism of deubiquitinase inhibition publication-title: eLife doi: 10.7554/eLife.13027 – volume: 111 start-page: 2984 year: 2014 end-page: 2989 ident: CR30 article-title: Crystal structure of the proteasomal deubiquitylation module Rpn8–Rpn11 publication-title: Proc. Natl Acad. Sci. USA doi: 10.1073/pnas.1400546111 – volume: 282 start-page: 22921 year: 2007 end-page: 22929 ident: CR38 article-title: ATP-induced structural transitions in PAN, the proteasome-regulatory ATPase complex in Archaea publication-title: J. Biol. Chem. doi: 10.1074/jbc.M702846200 – volume: 5 start-page: e18722 year: 2016 ident: CR53 article-title: Accelerated cryo-EM structure determination with parallelisation using GPUs in RELION-2 publication-title: eLife doi: 10.7554/eLife.18722 – volume: 298 start-page: 611 year: 2002 end-page: 615 ident: CR8 article-title: Role of Rpn11 metalloprotease in deubiquitination and degradation by the 26S proteasome publication-title: Science doi: 10.1126/science.1075898 – volume: 11 start-page: 63 year: 2014 end-page: 65 ident: CR55 article-title: Quantifying the local resolution of cryo-EM density maps publication-title: Nat. Methods doi: 10.1038/nmeth.2727 – ident: CR26 – volume: 23 start-page: 778 year: 2016 end-page: 785 ident: CR18 article-title: An atomic structure of the human 26S proteasome publication-title: Nat. Struct. Mol. Biol. doi: 10.1038/nsmb.3273 – volume: 9 year: 2018 ident: CR11 article-title: Structural mechanism for nucleotide-driven remodeling of the AAA-ATPase unfoldase in the activated human 26S proteasome publication-title: Nat. Commun. doi: 10.1038/s41467-018-03785-w – start-page: 213 year: 2010 end-page: 221 ident: CR57 article-title: PHENIX: a comprehensive Python-based system for macromolecular structure solution publication-title: Acta Crystallogr. D Biol. Crystallogr. – volume: 25 start-page: 1605 year: 2004 end-page: 1612 ident: CR58 article-title: UCSF Chimera—a visualization system for exploratory research and analysis publication-title: J. Comput. Chem. doi: 10.1002/jcc.20084 – volume: 41 start-page: 77 year: 2016 end-page: 93 ident: CR2 article-title: Gates, channels, and switches: elements of the proteasome machine publication-title: Trends Biochem. Sci. doi: 10.1016/j.tibs.2015.10.009 – volume: 357 start-page: 273 year: 2017 end-page: 279 ident: CR41 article-title: Ratchet-like polypeptide translocation mechanism of the AAA+ disaggregase Hsp104 publication-title: Science doi: 10.1126/science.aan1052 – volume: 18 year: 2017 ident: CR52 article-title: A deep convolutional neural network approach to single-particle recognition in cryo-electron microscopy publication-title: BMC Bioinformatics doi: 10.1186/s12859-017-1757-y – volume: 114 start-page: 1305 year: 2017 end-page: 1310 ident: CR13 article-title: Structural insights into the functional cycle of the ATPase module of the 26S proteasome publication-title: Proc. Natl Acad. Sci. USA doi: 10.1073/pnas.1621129114 – volume: 20 start-page: 513 year: 2012 end-page: 521 ident: CR34 article-title: The structure of the 26S proteasome subunit Rpn2 reveals its PC repeat domain as a closed toroid of two concentric α-helical rings publication-title: Structure doi: 10.1016/j.str.2011.12.015 – volume: 351 start-page: aad9421 year: 2016 ident: CR6 article-title: Rpn1 provides adjacent receptor sites for substrate binding and deubiquitination by the proteasome publication-title: Science doi: 10.1126/science.aad9421 – volume: 6 start-page: e25754 year: 2017 ident: CR40 article-title: Structure of a AAA+ unfoldase in the process of unfolding substrate publication-title: eLife doi: 10.7554/eLife.25754 – volume: 60 start-page: 2126 year: 2004 end-page: 2132 ident: CR56 article-title: Coot: model-building tools for molecular graphics publication-title: Acta Crystallogr. D Biol. Crystallogr. doi: 10.1107/S0907444904019158 – volume: 109 start-page: 14870 year: 2012 end-page: 14875 ident: CR20 article-title: Near-atomic resolution structural model of the yeast 26S proteasome publication-title: Proc. Natl Acad. Sci. USA doi: 10.1073/pnas.1213333109 – ident: CR27 – volume: 34 start-page: 473 year: 2009 end-page: 484 ident: CR28 article-title: Structural insights into the regulatory particle of the proteasome from publication-title: Mol. Cell doi: 10.1016/j.molcel.2009.04.021 – volume: 67 start-page: 799 year: 2017 end-page: 811.e8 ident: CR29 article-title: An AAA motor-driven mechanical switch in Rpn11 controls deubiquitination at the 26S proteasome publication-title: Mol. Cell doi: 10.1016/j.molcel.2017.07.023 – volume: 358 start-page: eaao0464 year: 2017 ident: CR39 article-title: Structure of the mitochondrial inner membrane AAA+ protease YME1 gives insight into substrate processing publication-title: Science doi: 10.1126/science.aao0464 – volume: 3 start-page: e1701726 year: 2017 ident: CR43 article-title: Structural pathway of regulated substrate transfer and threading through an Hsp100 disaggregase publication-title: Sci. Adv. doi: 10.1126/sciadv.1701726 – volume: 442 start-page: 270 year: 2006 end-page: 275 ident: CR45 article-title: Mechanism of DNA translocation in a replicative hexameric helicase publication-title: Nature doi: 10.1038/nature04943 – volume: 46 start-page: 54 year: 2012 end-page: 66 ident: CR17 article-title: Molecular model of the human 26S proteasome publication-title: Mol. Cell doi: 10.1016/j.molcel.2012.03.026 – volume: 118 start-page: 99 year: 2004 end-page: 110 ident: CR7 article-title: Multiubiquitin chain receptors define a layer of substrate selectivity in the ubiquitin-proteasome system publication-title: Cell doi: 10.1016/j.cell.2004.06.014 – volume: 348 start-page: 1250834 year: 2015 ident: CR25 article-title: Substrate degradation by the proteasome: a single-molecule kinetic analysis publication-title: Science doi: 10.1126/science.1250834 – volume: 372 start-page: 774 year: 2007 end-page: 797 ident: CR60 article-title: Inference of macromolecular assemblies from crystalline state publication-title: J. Mol. Biol. doi: 10.1016/j.jmb.2007.05.022 – volume: 6 start-page: e31324 year: 2017 ident: CR42 article-title: The AAA ATPase Vps4 binds ESCRT-III substrates through a repeating array of dipeptide-binding pockets publication-title: eLife doi: 10.7554/eLife.31324 – ident: CR59 – volume: 9 year: 2018 ident: CR35 article-title: Conformational switching in the coiled-coil domains of a proteasomal ATPase regulates substrate processing publication-title: Nat. Commun. doi: 10.1038/s41467-018-04731-6 – volume: 6 start-page: e24487 year: 2017 ident: CR44 article-title: Structural basis of protein translocation by the Vps4-Vta1 AAA ATPase publication-title: eLife doi: 10.7554/eLife.24487 – volume: 21 start-page: 220 year: 2014 end-page: 227 ident: CR31 article-title: Structure of the Rpn11–Rpn8 dimer reveals mechanisms of substrate deubiquitination during proteasomal degradation publication-title: Nat. Struct. Mol. Biol. doi: 10.1038/nsmb.2771 – volume: 12 start-page: e0182130 year: 2017 ident: CR54 article-title: Massively parallel unsupervised single-particle cryo-EM data clustering via statistical manifold learning publication-title: PLoS One doi: 10.1371/journal.pone.0182130 – volume: 67 start-page: 322 year: 2017 end-page: 333.e6 ident: CR5 article-title: Conformational landscape of the p28-bound human proteasome regulatory particle publication-title: Mol. Cell doi: 10.1016/j.molcel.2017.06.007 – volume: 139 start-page: 523 year: 2009 end-page: 534 ident: CR46 article-title: Running in reverse: the structural basis for translocation polarity in hexameric helicases publication-title: Cell doi: 10.1016/j.cell.2009.08.043 – volume: 23 start-page: 778 year: 2016 ident: 736_CR18 publication-title: Nat. Struct. Mol. Biol. doi: 10.1038/nsmb.3273 – volume: 114 start-page: 1305 year: 2017 ident: 736_CR13 publication-title: Proc. Natl Acad. Sci. USA doi: 10.1073/pnas.1621129114 – volume: 399 start-page: 215 year: 2005 ident: 736_CR23 publication-title: Methods Enzymol. doi: 10.1016/S0076-6879(05)99014-9 – volume: 152 start-page: 36 year: 2005 ident: 736_CR49 publication-title: J. Struct. Biol. doi: 10.1016/j.jsb.2005.07.007 – volume: 282 start-page: 22921 year: 2007 ident: 736_CR38 publication-title: J. Biol. Chem. doi: 10.1074/jbc.M702846200 – volume: 298 start-page: 611 year: 2002 ident: 736_CR8 publication-title: Science doi: 10.1126/science.1075898 – volume: 358 start-page: eaao0464 year: 2017 ident: 736_CR39 publication-title: Science doi: 10.1126/science.aao0464 – volume: 139 start-page: 744 year: 2009 ident: 736_CR36 publication-title: Cell doi: 10.1016/j.cell.2009.09.034 – volume: 6 start-page: e24487 year: 2017 ident: 736_CR44 publication-title: eLife doi: 10.7554/eLife.24487 – volume: 6 year: 2015 ident: 736_CR37 publication-title: Nat. Commun. doi: 10.1038/ncomms9520 – volume: 351 start-page: aad9421 year: 2016 ident: 736_CR6 publication-title: Science doi: 10.1126/science.aad9421 – volume: 24 start-page: 1301 year: 2018 ident: 736_CR12 publication-title: Cell Rep. doi: 10.1016/j.celrep.2018.07.004 – volume: 110 start-page: 7264 year: 2013 ident: 736_CR21 publication-title: Proc. Natl Acad. Sci. USA doi: 10.1073/pnas.1305782110 – volume: 113 start-page: 7816 year: 2016 ident: 736_CR14 publication-title: Proc. Natl Acad. Sci. USA doi: 10.1073/pnas.1608050113 – start-page: 213 volume-title: Acta Crystallogr. D Biol. Crystallogr. year: 2010 ident: 736_CR57 – volume: 60 start-page: 2126 year: 2004 ident: 736_CR56 publication-title: Acta Crystallogr. D Biol. Crystallogr. doi: 10.1107/S0907444904019158 – ident: 736_CR4 doi: 10.1038/386463a0 – volume: 3 start-page: e1701726 year: 2017 ident: 736_CR43 publication-title: Sci. Adv. doi: 10.1126/sciadv.1701726 – volume: 46 start-page: 54 year: 2012 ident: 736_CR17 publication-title: Mol. Cell doi: 10.1016/j.molcel.2012.03.026 – volume: 67 start-page: 799 year: 2017 ident: 736_CR29 publication-title: Mol. Cell doi: 10.1016/j.molcel.2017.07.023 – volume: 25 start-page: 1605 year: 2004 ident: 736_CR58 publication-title: J. Comput. Chem. doi: 10.1002/jcc.20084 – volume: 87 start-page: 697 year: 2018 ident: 736_CR3 publication-title: Annu. Rev. Biochem. doi: 10.1146/annurev-biochem-062917-011931 – volume: 5 start-page: e18722 year: 2016 ident: 736_CR53 publication-title: eLife doi: 10.7554/eLife.18722 – volume: 357 start-page: 273 year: 2017 ident: 736_CR41 publication-title: Science doi: 10.1126/science.aan1052 – volume: 11 start-page: 63 year: 2014 ident: 736_CR55 publication-title: Nat. Methods doi: 10.1038/nmeth.2727 – volume: 111 start-page: 2984 year: 2014 ident: 736_CR30 publication-title: Proc. Natl Acad. Sci. USA doi: 10.1073/pnas.1400546111 – volume: 442 start-page: 270 year: 2006 ident: 736_CR45 publication-title: Nature doi: 10.1038/nature04943 – volume: 144 start-page: 526 year: 2011 ident: 736_CR9 publication-title: Cell doi: 10.1016/j.cell.2011.02.005 – volume: 8 start-page: 439 year: 2001 ident: 736_CR24 publication-title: Mol. Cell doi: 10.1016/S1097-2765(01)00308-2 – volume: 9 year: 2018 ident: 736_CR11 publication-title: Nat. Commun. doi: 10.1038/s41467-018-03785-w – volume: 139 start-page: 523 year: 2009 ident: 736_CR46 publication-title: Cell doi: 10.1016/j.cell.2009.08.043 – volume: 151 start-page: 41 year: 2005 ident: 736_CR48 publication-title: J. Struct. Biol. doi: 10.1016/j.jsb.2005.03.010 – volume: 21 start-page: 220 year: 2014 ident: 736_CR31 publication-title: Nat. Struct. Mol. Biol. doi: 10.1038/nsmb.2771 – volume: 15 start-page: 1223 year: 2008 ident: 736_CR33 publication-title: Nat. Struct. Mol. Biol. doi: 10.1038/nsmb.1501 – volume: 12 start-page: e0182130 year: 2017 ident: 736_CR54 publication-title: PLoS One doi: 10.1371/journal.pone.0182130 – ident: 736_CR26 doi: 10.1093/emboj/16.19.5847 – volume: 14 start-page: 331 year: 2017 ident: 736_CR50 publication-title: Nat. Methods doi: 10.1038/nmeth.4193 – volume: 109 start-page: 1380 year: 2012 ident: 736_CR15 publication-title: Proc. Natl Acad. Sci. USA doi: 10.1073/pnas.1120559109 – volume: 34 start-page: 473 year: 2009 ident: 736_CR28 publication-title: Mol. Cell doi: 10.1016/j.molcel.2009.04.021 – volume: 67 start-page: 322 year: 2017 ident: 736_CR5 publication-title: Mol. Cell doi: 10.1016/j.molcel.2017.06.007 – ident: 736_CR59 – volume: 26 start-page: 869 year: 2016 ident: 736_CR1 publication-title: Cell Res. doi: 10.1038/cr.2016.86 – volume: 113 start-page: 2642 year: 2016 ident: 736_CR19 publication-title: Proc. Natl Acad. Sci. USA doi: 10.1073/pnas.1601561113 – volume: 109 start-page: 14870 year: 2012 ident: 736_CR20 publication-title: Proc. Natl Acad. Sci. USA doi: 10.1073/pnas.1213333109 – volume: 46 start-page: 3553 year: 2007 ident: 736_CR47 publication-title: Biochemistry doi: 10.1021/bi061994u – volume: 348 start-page: 1250834 year: 2015 ident: 736_CR25 publication-title: Science doi: 10.1126/science.1250834 – volume: 41 start-page: 77 year: 2016 ident: 736_CR2 publication-title: Trends Biochem. Sci. doi: 10.1016/j.tibs.2015.10.009 – volume: 5 start-page: e13027 year: 2016 ident: 736_CR32 publication-title: eLife doi: 10.7554/eLife.13027 – ident: 736_CR27 doi: 10.1038/35040607 – volume: 20 start-page: 513 year: 2012 ident: 736_CR34 publication-title: Structure doi: 10.1016/j.str.2011.12.015 – volume: 372 start-page: 774 year: 2007 ident: 736_CR60 publication-title: J. Mol. Biol. doi: 10.1016/j.jmb.2007.05.022 – ident: 736_CR22 – volume: 482 start-page: 186 year: 2012 ident: 736_CR16 publication-title: Nature doi: 10.1038/nature10774 – volume: 6 start-page: e31324 year: 2017 ident: 736_CR42 publication-title: eLife doi: 10.7554/eLife.31324 – volume: 193 start-page: 1 year: 2016 ident: 736_CR51 publication-title: J. Struct. Biol. doi: 10.1016/j.jsb.2015.11.003 – volume: 6 start-page: e25754 year: 2017 ident: 736_CR40 publication-title: eLife doi: 10.7554/eLife.25754 – volume: 18 year: 2017 ident: 736_CR52 publication-title: BMC Bioinformatics doi: 10.1186/s12859-017-1757-y – volume: 118 start-page: 99 year: 2004 ident: 736_CR7 publication-title: Cell doi: 10.1016/j.cell.2004.06.014 – volume: 9 year: 2018 ident: 736_CR35 publication-title: Nat. Commun. doi: 10.1038/s41467-018-04731-6 – volume: 113 start-page: 12991 year: 2016 ident: 736_CR10 publication-title: Proc. Natl Acad. Sci. USA doi: 10.1073/pnas.1614614113 |
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| Snippet | The proteasome is an ATP-dependent, 2.5-megadalton molecular machine that is responsible for selective protein degradation in eukaryotic cells. Here we present... The proteasome is an ATP-dependent, 2.5-megadalton machine responsible for selective protein degradation in eukaryotic cells. Here we present cryo-EM... |
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| SubjectTerms | 101/28 631/45/468 631/535/1258/1259 631/80/474/2085 82/83 Adenosine diphosphate Adenosine triphosphatase Adenosine Triphosphatases - metabolism Adenosine Triphosphate - metabolism Allosteric Regulation ATP ATPases Automation Binding sites Biodegradation Cell cycle Cryoelectron Microscopy Electron microscopy Holoenzymes - chemistry Holoenzymes - metabolism Holoenzymes - ultrastructure Humanities and Social Sciences Humans Hydrolysis Microscopy Models, Molecular Molecular machines multidisciplinary Proteasome 26S Proteasome Endopeptidase Complex - chemistry Proteasome Endopeptidase Complex - metabolism Proteasome Endopeptidase Complex - ultrastructure Protein Conformation Protein research Protein Structure, Quaternary Protein Unfolding Proteins Proteolysis Science Science (multidisciplinary) Substrate Specificity Substrates Synchronism Synchronization Translocation Ubiquitin Ubiquitin-proteasome system Ubiquitination |
| Title | Cryo-EM structures and dynamics of substrate-engaged human 26S proteasome |
| URI | https://link.springer.com/article/10.1038/s41586-018-0736-4 https://www.ncbi.nlm.nih.gov/pubmed/30479383 https://www.proquest.com/docview/2166932464 https://www.proquest.com/docview/2138638814 https://pubmed.ncbi.nlm.nih.gov/PMC6370054 |
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