Reconfiguration of the proteasome during chaperone-mediated assembly
The proteasome degrades ubiquitin-conjugated substrates; here, structural and functional insights from studies in yeast reveal that it is reconfigured during chaperone-mediated assembly. Proteasome structure and function The proteasome is a protein complex that degrades ubiquitin-conjugated substrat...
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| Published in | Nature (London) Vol. 497; no. 7450; pp. 512 - 516 |
|---|---|
| Main Authors | , , , , , , , , , , , , |
| Format | Journal Article |
| Language | English |
| Published |
London
Nature Publishing Group UK
23.05.2013
Nature Publishing Group |
| Subjects | |
| Online Access | Get full text |
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| Abstract | The proteasome degrades ubiquitin-conjugated substrates; here, structural and functional insights from studies in yeast reveal that it is reconfigured during chaperone-mediated assembly.
Proteasome structure and function
The proteasome is a protein complex that degrades ubiquitin-conjugated substrates. The 26S proteasome consists of a core particle (CP) and a regulatory particle (RP) formed of a base and lid. In this study, Daniel Finley and colleagues present structural and functional insights into the assembly of the base–CP complex.
The proteasomal ATPase ring, comprising Rpt1–Rpt6, associates with the heptameric α-ring of the proteasome core particle (CP) in the mature proteasome, with the Rpt carboxy-terminal tails inserting into pockets of the α-ring
1
,
2
,
3
,
4
. Rpt ring assembly is mediated by four chaperones, each binding a distinct Rpt subunit
5
,
6
,
7
,
8
,
9
,
10
. Here we report that the base subassembly of the
Saccharomyces cerevisiae
proteasome, which includes the Rpt ring, forms a high-affinity complex with the CP. This complex is subject to active dissociation by the chaperones Hsm3, Nas6 and Rpn14. Chaperone-mediated dissociation was abrogated by a non-hydrolysable ATP analogue, indicating that chaperone action is coupled to nucleotide hydrolysis by the Rpt ring. Unexpectedly, synthetic Rpt tail peptides bound α-pockets with poor specificity, except for Rpt6, which uniquely bound the α2/α3-pocket. Although the Rpt6 tail is not visualized within an α-pocket in mature proteasomes
2
,
3
,
4
, it inserts into the α2/α3-pocket in the base–CP complex and is important for complex formation. Thus, the Rpt–CP interface is reconfigured when the lid complex joins the nascent proteasome to form the mature holoenzyme. |
|---|---|
| AbstractList | The proteasomal ATPase ring, comprising Rpt1-Rpt6, associates with the heptameric α-ring of the proteasome core particle (CP) in the mature proteasome, with the Rpt carboxy-terminal tails inserting into pockets of the α-ring. Rpt ring assembly is mediated by four chaperones, each binding a distinct Rpt subunit. Here we report that the base subassembly of the Saccharomyces cerevisiae proteasome, which includes the Rpt ring, forms a high-affinity complex with the CP. This complex is subject to active dissociation by the chaperones Hsm3, Nas6 and Rpn14. Chaperone-mediated dissociation was abrogated by a non-hydrolysable ATP analogue, indicating that chaperone action is coupled to nucleotide hydrolysis by the Rpt ring. Unexpectedly, synthetic Rpt tail peptides bound α-pockets with poor specificity, except for Rpt6, which uniquely bound the α2/α3-pocket. Although the Rpt6 tail is not visualized within an α-pocket in mature proteasomes, it inserts into the α2/α3-pocket in the base-CP complex and is important for complex formation. Thus, the Rpt-CP interface is reconfigured when the lid complex joins the nascent proteasome to form the mature holoenzyme. The proteasomal ATPase ring, comprising Rpt1-Rpt6, associates with the heptameric α-ring of the proteasome core particle (CP) in the mature proteasome, with the Rpt carboxy-terminal tails inserting into pockets of the α-ring. Rpt ring assembly is mediated by four chaperones, each binding a distinct Rpt subunit. Here we report that the base subassembly of the Saccharomyces cerevisiae proteasome, which includes the Rpt ring, forms a high-affinity complex with the CP. This complex is subject to active dissociation by the chaperones Hsm3, Nas6 and Rpn14. Chaperone-mediated dissociation was abrogated by a non-hydrolysable ATP analogue, indicating that chaperone action is coupled to nucleotide hydrolysis by the Rpt ring. Unexpectedly, synthetic Rpt tail peptides bound α-pockets with poor specificity, except for Rpt6, which uniquely bound the α2/α3-pocket. Although the Rpt6 tail is not visualized within an α-pocket in mature proteasomes, it inserts into the α2/α3-pocket in the base-CP complex and is important for complex formation. Thus, the Rpt-CP interface is reconfigured when the lid complex joins the nascent proteasome to form the mature holoenzyme.The proteasomal ATPase ring, comprising Rpt1-Rpt6, associates with the heptameric α-ring of the proteasome core particle (CP) in the mature proteasome, with the Rpt carboxy-terminal tails inserting into pockets of the α-ring. Rpt ring assembly is mediated by four chaperones, each binding a distinct Rpt subunit. Here we report that the base subassembly of the Saccharomyces cerevisiae proteasome, which includes the Rpt ring, forms a high-affinity complex with the CP. This complex is subject to active dissociation by the chaperones Hsm3, Nas6 and Rpn14. Chaperone-mediated dissociation was abrogated by a non-hydrolysable ATP analogue, indicating that chaperone action is coupled to nucleotide hydrolysis by the Rpt ring. Unexpectedly, synthetic Rpt tail peptides bound α-pockets with poor specificity, except for Rpt6, which uniquely bound the α2/α3-pocket. Although the Rpt6 tail is not visualized within an α-pocket in mature proteasomes, it inserts into the α2/α3-pocket in the base-CP complex and is important for complex formation. Thus, the Rpt-CP interface is reconfigured when the lid complex joins the nascent proteasome to form the mature holoenzyme. The proteasome degrades ubiquitin-conjugated substrates; here, structural and functional insights from studies in yeast reveal that it is reconfigured during chaperone-mediated assembly. Proteasome structure and function The proteasome is a protein complex that degrades ubiquitin-conjugated substrates. The 26S proteasome consists of a core particle (CP) and a regulatory particle (RP) formed of a base and lid. In this study, Daniel Finley and colleagues present structural and functional insights into the assembly of the base–CP complex. The proteasomal ATPase ring, comprising Rpt1–Rpt6, associates with the heptameric α-ring of the proteasome core particle (CP) in the mature proteasome, with the Rpt carboxy-terminal tails inserting into pockets of the α-ring 1 , 2 , 3 , 4 . Rpt ring assembly is mediated by four chaperones, each binding a distinct Rpt subunit 5 , 6 , 7 , 8 , 9 , 10 . Here we report that the base subassembly of the Saccharomyces cerevisiae proteasome, which includes the Rpt ring, forms a high-affinity complex with the CP. This complex is subject to active dissociation by the chaperones Hsm3, Nas6 and Rpn14. Chaperone-mediated dissociation was abrogated by a non-hydrolysable ATP analogue, indicating that chaperone action is coupled to nucleotide hydrolysis by the Rpt ring. Unexpectedly, synthetic Rpt tail peptides bound α-pockets with poor specificity, except for Rpt6, which uniquely bound the α2/α3-pocket. Although the Rpt6 tail is not visualized within an α-pocket in mature proteasomes 2 , 3 , 4 , it inserts into the α2/α3-pocket in the base–CP complex and is important for complex formation. Thus, the Rpt–CP interface is reconfigured when the lid complex joins the nascent proteasome to form the mature holoenzyme. The proteasomal ATPase ring, comprising Rpt1-Rpt6, associates with the heptameric α ring of the proteasome core particle (CP) in the mature proteasome, with the Rpt C-terminal tails inserting into pockets of the α ring 1 – 4 . Rpt ring assembly is mediated by four chaperones, each binding a distinct Rpt subunit 5 – 10 . We report that the base subassembly of the proteasome, which includes the Rpt ring, forms a high affinity complex with the CP. This complex is subject to active dissociation by the chaperones Hsm3, Nas6, and Rpn14. Chaperone-mediated dissociation was abrogated by a nonhydrolyzable ATP analog, indicating that chaperone action is coupled to nucleotide hydrolysis by the Rpt ring. Unexpectedly, synthetic Rpt tail peptides bound α pockets with poor specificity, except for Rpt6, which uniquely bound the α2/α3 pocket. Although the Rpt6 tail is not visualized within an α pocket in mature proteasomes 2 – 4 , it inserts into the α2/α3 pocket in the base-CP complex and is important for complex formation. Thus, the Rpt-CP interface is reconfigured when the lid complex joins the nascent proteasome to form the mature holoenzyme. The proteasome degrades ubiquitin-conjugated substrates; here, structural and functional insights from studies in yeast reveal that it is reconfigured during chaperone-mediated assembly. The proteasomal ATPase ring, comprising Rpt1-Rpt6, associates with the heptameric a-ring of the proteasome core particle (CP) in the mature proteasome, with the Rpt carboxy-terminal tails inserting into pockets of the a-ring1-4. Rpt ring assembly is mediated by four chaperones, each binding a distinct Rpt subunit5-10. Here we report that the base subassembly of the Saccharomyces cerevisiae proteasome, which includes the Rpt ring, forms a high-affinity complex with the CP. This complex is subject to active dissociation by the chaperones Hsm3, Nas6 and Rpn14. Chaperone-mediated dissociation was abrogated by a non-hydrolysable ATP analogue, indicating that chaperone action is coupled to nucleotide hydrolysis by the Rpt ring. Unexpectedly, synthetic Rpt tail peptides bound a-pockets with poor specificity, except for Rpt6, which uniquely bound the a2/a3-pocket. Although the Rpt6 tail is not visualized within an a-pocket in mature proteasomes2-4, it inserts into the a2/a3-pocket in the base-CP complex and is important for complex formation. Thus, the Rpt-CP interface is reconfigured when the lid complex joins the nascent proteasome to form the mature holoenzyme. [PUBLICATION ABSTRACT] |
| Audience | Academic |
| Author | Lovell, Scott Park, Soyeon Tian, Geng Zolkiewski, Michal Roelofs, Jeroen Coffino, Philip Battaile, Kevin P. Cheng, Yifan Li, Xueming Hoyt, Martin A. Kim, Ho Min Finley, Daniel Singh, Chingakham Ranjit |
| AuthorAffiliation | 7 Protein Structure Laboratory, Del Shankel Structural Biology Center, University of Kansas, Lawrence, KS 66047 2 MCD Biology, University of Colorado Boulder, Boulder, CO 80309 5 Division of Biology, Kansas State University, 338 Ackert Hall, Manhattan, KS 66506 1 Dept. of Cell Biology, Harvard Medical School, 240 Longwood Ave., Boston, MA 02115 3 The W.M. Keck Advanced Microscopy Laboratory, Department of Biochemistry and Biophysics, University of California San Francisco, 600 16th Street, San Francisco, CA 94158 8 IMCA-CAT Hauptman-Woodward Medical Research Institute, 9700 South Cass Avenue, Building 435A, Argonne, Illinois, 60439 9 Department of Biochemistry, Kansas State University, 176 Chalmers Hall, Manhattan Kansas 66506 6 Department of Microbiology and Immunology, University of California San Francisco, 513 Parnassus Avenue, San Francisco, CA 94143 |
| AuthorAffiliation_xml | – name: 2 MCD Biology, University of Colorado Boulder, Boulder, CO 80309 – name: 3 The W.M. Keck Advanced Microscopy Laboratory, Department of Biochemistry and Biophysics, University of California San Francisco, 600 16th Street, San Francisco, CA 94158 – name: 6 Department of Microbiology and Immunology, University of California San Francisco, 513 Parnassus Avenue, San Francisco, CA 94143 – name: 7 Protein Structure Laboratory, Del Shankel Structural Biology Center, University of Kansas, Lawrence, KS 66047 – name: 8 IMCA-CAT Hauptman-Woodward Medical Research Institute, 9700 South Cass Avenue, Building 435A, Argonne, Illinois, 60439 – name: 1 Dept. of Cell Biology, Harvard Medical School, 240 Longwood Ave., Boston, MA 02115 – name: 5 Division of Biology, Kansas State University, 338 Ackert Hall, Manhattan, KS 66506 – name: 9 Department of Biochemistry, Kansas State University, 176 Chalmers Hall, Manhattan Kansas 66506 |
| Author_xml | – sequence: 1 givenname: Soyeon surname: Park fullname: Park, Soyeon organization: Department of Cell Biology, Harvard Medical School, 240 Longwood Avenue, Boston, Massachusetts 02115, USA, MCD Biology, University of Colorado Boulder – sequence: 2 givenname: Xueming surname: Li fullname: Li, Xueming organization: Department of Biochemistry and Biophysics, The W.M. Keck Advanced Microscopy Laboratory, University of California San Francisco, 600 16th Street, San Francisco, California 94158, USA – sequence: 3 givenname: Ho Min surname: Kim fullname: Kim, Ho Min organization: Department of Biochemistry and Biophysics, The W.M. Keck Advanced Microscopy Laboratory, University of California San Francisco, 600 16th Street, San Francisco, California 94158, USA, Present address: Graduate School of Medical Science and Engineering, Korea Advanced Institute of Science and Technology, Daejeon 305-701, Korea – sequence: 4 givenname: Chingakham Ranjit surname: Singh fullname: Singh, Chingakham Ranjit organization: Division of Biology, Kansas State University, 338 Ackert Hall, Manhattan, Kansas 66506, USA – sequence: 5 givenname: Geng surname: Tian fullname: Tian, Geng organization: Department of Cell Biology, Harvard Medical School, 240 Longwood Avenue, Boston, Massachusetts 02115, USA – sequence: 6 givenname: Martin A. surname: Hoyt fullname: Hoyt, Martin A. organization: Department of Microbiology and Immunology, University of California San Francisco, 513 Parnassus Avenue, San Francisco, California 94143, USA – sequence: 7 givenname: Scott surname: Lovell fullname: Lovell, Scott organization: Protein Structure Laboratory, Del Shankel Structural Biology Center, University of Kansas – sequence: 8 givenname: Kevin P. surname: Battaile fullname: Battaile, Kevin P. organization: IMCA-CAT Hauptman-Woodward Medical Research Institute, 9700 South Cass Avenue, Building 435A, Argonne, Illinois 60439, USA – sequence: 9 givenname: Michal surname: Zolkiewski fullname: Zolkiewski, Michal organization: Department of Biochemistry, Kansas State University, 176 Chalmers Hall, Manhattan, Kansas 66506, USA – sequence: 10 givenname: Philip surname: Coffino fullname: Coffino, Philip organization: Department of Microbiology and Immunology, University of California San Francisco, 513 Parnassus Avenue, San Francisco, California 94143, USA – sequence: 11 givenname: Jeroen surname: Roelofs fullname: Roelofs, Jeroen email: jroelofs@ksu.edu organization: Division of Biology, Kansas State University, 338 Ackert Hall, Manhattan, Kansas 66506, USA – sequence: 12 givenname: Yifan surname: Cheng fullname: Cheng, Yifan email: ycheng@ucsf.edu organization: Department of Biochemistry and Biophysics, The W.M. Keck Advanced Microscopy Laboratory, University of California San Francisco, 600 16th Street, San Francisco, California 94158, USA – sequence: 13 givenname: Daniel surname: Finley fullname: Finley, Daniel email: daniel_finley@hms.harvard.edu organization: Department of Cell Biology, Harvard Medical School, 240 Longwood Avenue, Boston, Massachusetts 02115, USA |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/23644457$$D View this record in MEDLINE/PubMed |
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| ContentType | Journal Article |
| Copyright | Springer Nature Limited 2013 COPYRIGHT 2013 Nature Publishing Group Copyright Nature Publishing Group May 23, 2013 |
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| DOI | 10.1038/nature12123 |
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| Notes | ObjectType-Article-2 SourceType-Scholarly Journals-1 ObjectType-Feature-1 content type line 14 ObjectType-Article-1 ObjectType-Feature-2 content type line 23 These authors contributed equally to this work. Present address: Graduate School of Medical Science and Engineering, Korea Advanced Institute of Science and Technology, Daejeon 305-701, Korea |
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| References_xml | – reference: ForsterAMastersEIWhitbyFGRobinsonHHillCPThe 1.9 Å structure of a proteasome-11S activator complex and implications for proteasome-PAN/PA700 interactionsMol. Cell20051858959910.1016/j.molcel.2005.04.016 – reference: SmithDMDocking of the proteasomal ATPases’ carboxyl termini in the 20S proteasome’s α ring opens the gate for substrate entryMol. Cell2007277317441:CAS:528:DC%2BD2sXhtFWlsL7J10.1016/j.molcel.2007.06.033 – reference: BarraultMBDual functions of the Hsm3 protein in chaperoning and scaffolding regulatory particle subunits during the proteasome assemblyProc. Natl Acad. Sci. USA2012109E1001E101010.1073/pnas.1116538109 – reference: KusmierczykARKunjappuMJFunakoshiMHochstrasserMA multimeric assembly factor controls the formation of alternative 20S proteasomesNature Struct. Mol. Biol.2008152372441:CAS:528:DC%2BD1cXislKmtbg%3D10.1038/nsmb.1389 – reference: PathareGRThe proteasomal subunit Rpn6 is a molecular clamp holding the core and regulatory subcomplexes togetherProc. Natl Acad. Sci. USA20121091491542012PNAS..109..149P1:CAS:528:DC%2BC38XhsVehsLY%3D10.1073/pnas.1117648108 – reference: FunakoshiMTomkoRJJrKobayashiHHochstrasserMMultiple assembly chaperones govern biogenesis of the proteasome regulatory particle baseCell20091378878991:CAS:528:DC%2BD1MXosVCltbo%3D10.1016/j.cell.2009.04.061 – reference: TomkoRJJrFunakoshiMSchneiderKWangJHochstrasserMHeterohexameric ring arrangement of the eukaryotic proteasomal ATPases: implications for proteasome structure and assemblyMol. Cell2010383934031:CAS:528:DC%2BC3cXms1alsb0%3D10.1016/j.molcel.2010.02.035 – reference: TianGAn asymmetric interface between the regulatory particle and core particle of the proteasomeNature Struct. Mol. Biol.201118125912671:CAS:528:DC%2BC3MXhtl2gs7fE10.1038/nsmb.2147 – reference: KanekoTAssembly pathway of the mammalian proteasome base subcomplex is mediated by multiple specific chaperonesCell20091379149251:CAS:528:DC%2BD1MXosVCltbg%3D10.1016/j.cell.2009.05.008 – reference: ParkSHexameric assembly of the proteasomal ATPases is templated through their C terminiNature20094598668702009Natur.459..866P1:CAS:528:DC%2BD1MXntV2jsLk%3D10.1038/nature08065 – reference: SmithDMFragaHReisCKafriGGoldbergALATP binds to proteasomal ATPases in pairs with distinct functional effects, implying an ordered reaction cycleCell20111445265381:CAS:528:DC%2BC3MXit1Gqu7o%3D10.1016/j.cell.2011.02.005 – reference: SmithDMATP binding to PAN or the 26S ATPases causes association with the 20S proteasome, gate opening, and translocation of unfolded proteinsMol. Cell2005206876981:CAS:528:DC%2BD2MXhtleqtb%2FO10.1016/j.molcel.2005.10.019 – reference: Le TallecBBarraultMBGueroisRCarreTPeyrocheAHsm3/S5b participates in the assembly pathway of the 19S regulatory particle of the proteasomeMol. Cell2009333893991:CAS:528:DC%2BD1MXltFSnuro%3D10.1016/j.molcel.2009.01.010 – reference: LaskerKMolecular architecture of the 26S proteasome holocomplex determined by an integrative approachProc. Natl Acad. Sci. USA2012109138013872012PNAS..109.1380L1:CAS:528:DC%2BC38Xitlagsro%3D10.1073/pnas.1120559109 – reference: NakamuraYStructural basis for the recognition between the regulatory particles Nas6 and Rpt3 of the yeast 26S proteasomeBiochem. Biophys. Res. Commun.20073595035091:CAS:528:DC%2BD2sXmsFylu7o%3D10.1016/j.bbrc.2007.05.138 – reference: RablJMechanism of gate opening in the 20S proteasome by the proteasomal ATPasesMol. Cell2008303603681:CAS:528:DC%2BD1cXmtFaktLk%3D10.1016/j.molcel.2008.03.004 – reference: GhaemmaghamiSGlobal analysis of protein expression in yeastNature20034257377412003Natur.425..737G1:CAS:528:DC%2BD3sXotV2iu7c%3D10.1038/nature02046 – reference: TakagiKStructural basis for specific recognition of Rpt1, an ATPase subunit of 26S proteasome, by proteasome-dedicated chaperone Hsm3pJ. Biol. Chem.201228712172121821:CAS:528:DC%2BC38XltVykt74%3D10.1074/jbc.M112.345876 – reference: BeckFNear-atomic resolution structural model of the yeast 26S proteasomeProc. Natl Acad. Sci. USA201210914870148752012PNAS..10914870B1:CAS:528:DC%2BC38XhsVelsrjL10.1073/pnas.1213333109 – reference: SaekiYTohEAKudoTKawamuraHTanakaKMultiple proteasome-interacting proteins assist the assembly of the yeast 19S regulatory particleCell20091379009131:CAS:528:DC%2BD1MXosVCltbs%3D10.1016/j.cell.2009.05.005 – reference: RoelofsJChaperone-mediated pathway of proteasome regulatory particle assemblyNature20094598618652009Natur.459..861R1:CAS:528:DC%2BD1MXntV2jsrc%3D10.1038/nature08063 – reference: ParkSKimWTianGGygiSPFinleyDStructural defects in the RP-CP interface induce a novel proteasome stress responseJ. Biol. Chem.201128636652366661:CAS:528:DC%2BC3MXhtlSqtLzK10.1074/jbc.M111.285924 – reference: LanderGCComplete subunit architecture of the proteasome regulatory particleNature20124821861912012Natur.482..186L1:CAS:528:DC%2BC38Xls1ShsA%3D%3D10.1038/nature10774 – reference: Kish-Trier, E. & Hill, C. P. Structural biology of the proteasome. Ann. Rev.. 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| Snippet | The proteasome degrades ubiquitin-conjugated substrates; here, structural and functional insights from studies in yeast reveal that it is reconfigured during... The proteasomal ATPase ring, comprising Rpt1-Rpt6, associates with the heptameric α-ring of the proteasome core particle (CP) in the mature proteasome, with... The proteasomal ATPase ring, comprising Rpt1-Rpt6, associates with the heptameric a-ring of the proteasome core particle (CP) in the mature proteasome, with... The proteasomal ATPase ring, comprising Rpt1-Rpt6, associates with the heptameric α ring of the proteasome core particle (CP) in the mature proteasome, with... |
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| SubjectTerms | 631/45 631/535/1258 Adenosine triphosphatase Adenosine Triphosphatases - chemistry Adenosine Triphosphatases - genetics Adenosine Triphosphatases - metabolism Adenosine Triphosphate - metabolism ATPases Binding Sites Brewer's yeast Carrier Proteins - metabolism Cryoelectron Microscopy Enzymes Holoenzymes - chemistry Holoenzymes - metabolism Humanities and Social Sciences Hydrolysis letter Models, Molecular Molecular chaperones Molecular Chaperones - metabolism multidisciplinary Peptides Physiological aspects Proteasome Endopeptidase Complex - chemistry Proteasome Endopeptidase Complex - genetics Proteasome Endopeptidase Complex - metabolism Protein Conformation Recombinant Fusion Proteins - chemistry Recombinant Fusion Proteins - genetics Recombinant Fusion Proteins - metabolism Saccharomyces cerevisiae - enzymology Saccharomyces cerevisiae - genetics Saccharomyces cerevisiae - growth & development Saccharomyces cerevisiae - metabolism Saccharomyces cerevisiae Proteins - chemistry Saccharomyces cerevisiae Proteins - genetics Saccharomyces cerevisiae Proteins - metabolism Science Ubiquitin Ubiquitin-proteasome system Yeast |
| Title | Reconfiguration of the proteasome during chaperone-mediated assembly |
| URI | https://link.springer.com/article/10.1038/nature12123 https://www.ncbi.nlm.nih.gov/pubmed/23644457 https://www.proquest.com/docview/1366376950 https://www.proquest.com/docview/1355476807 https://pubmed.ncbi.nlm.nih.gov/PMC3687086 |
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