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Disassembly of the self-assembled, double-ring structure of proteasome α7 homo-tetradecamer by α6.

Ishii K, Noda M, Yagi H, Thammaporn R, Seetaha S, Satoh T, Kato K, Uchiyama S
Sci Rep 5 18167 (2015)
Cited: 22 times
EuropePMC logo PMID: 26657688

Abstract

The 20S core particle of the eukaryotic proteasome is composed of two α- and two β-rings, each of which is a hetero-heptamer composed of seven homologous but distinct subunits. Although formation of the eukaryotic proteasome is a highly ordered process assisted by assembly chaperones, α7, an α-ring component, has the unique property of self-assembling into a homo-tetradecamer. We used biophysical methods to characterize the oligomeric states of this proteasome subunit and its interaction with α6, which makes direct contacts with α7 in the proteasome α-ring. We determined a crystal structure of the α7 tetradecamer, which has a double-ring structure. Sedimentation velocity analytical ultracentrifugation and mass spectrometric analysis under non-denaturing conditions revealed that α7 exclusively exists as homo-tetradecamer in solution and that its double-ring structure is disassembled upon the addition of α6, resulting in a 1:7 hetero-octameric α6-α7 complex. Our findings suggest that proteasome formation involves the disassembly of non-native oligomers, which are assembly intermediates.

Reviews - 5dsv mentioned but not cited (2)

  1. Stereochemistry and Validation of Macromolecular Structures. Wlodawer A. Methods Mol Biol 1607 595-610 (2017)
  2. Structural insights on the dynamics of proteasome formation. Kato K, Satoh T. Biophys Rev 10 597-604 (2018)

Articles - 5dsv mentioned but not cited (4)

  1. Disassembly of the self-assembled, double-ring structure of proteasome α7 homo-tetradecamer by α6. Ishii K, Noda M, Yagi H, Thammaporn R, Seetaha S, Satoh T, Kato K, Uchiyama S. Sci Rep 5 18167 (2015)
  2. Two-step process for disassembly mechanism of proteasome α7 homo-tetradecamer by α6 revealed by high-speed atomic force microscopy. Kozai T, Sekiguchi T, Satoh T, Yagi H, Kato K, Uchihashi T. Sci Rep 7 15373 (2017)
  3. Mutational and Combinatorial Control of Self-Assembling and Disassembling of Human Proteasome α Subunits. Sekiguchi T, Satoh T, Kurimoto E, Song C, Kozai T, Watanabe H, Ishii K, Yagi H, Yanaka S, Uchiyama S, Uchihashi T, Murata K, Kato K. Int J Mol Sci 20 E2308 (2019)
  4. Structural Fluctuations of the Human Proteasome α7 Homo-Tetradecamer Double Ring Imply the Proteasomal α-Ring Assembly Mechanism. Song C, Satoh T, Sekiguchi T, Kato K, Murata K. Int J Mol Sci 22 4519 (2021)


Reviews citing this publication (2)

  1. Proteasome Structure and Assembly. Budenholzer L, Cheng CL, Li Y, Hochstrasser M. J Mol Biol 429 3500-3524 (2017)
  2. Dynamic Regulation of the 26S Proteasome: From Synthesis to Degradation. Marshall RS, Vierstra RD. Front Mol Biosci 6 40 (2019)

Articles citing this publication (14)

  1. Dynamic structural states of ClpB involved in its disaggregation function. Uchihashi T, Watanabe YH, Nakazaki Y, Yamasaki T, Watanabe H, Maruno T, Ishii K, Uchiyama S, Song C, Murata K, Iino R, Ando T. Nat Commun 9 2147 (2018)
  2. Analytical ultracentrifugation with fluorescence detection system reveals differences in complex formation between recombinant human TNF and different biological TNF antagonists in various environments. Krayukhina E, Noda M, Ishii K, Maruno T, Wakabayashi H, Tada M, Suzuki T, Ishii-Watabe A, Kato M, Uchiyama S. MAbs 9 664-679 (2017)
  3. PAC1-PAC2 proteasome assembly chaperone retains the core α4-α7 assembly intermediates in the cytoplasm. Wu W, Sahara K, Hirayama S, Zhao X, Watanabe A, Hamazaki J, Yashiroda H, Murata S. Genes Cells 23 839-848 (2018)
  4. Molecular and Structural Basis of the Proteasome α Subunit Assembly Mechanism Mediated by the Proteasome-Assembling Chaperone PAC3-PAC4 Heterodimer. Satoh T, Yagi-Utsumi M, Okamoto K, Kurimoto E, Tanaka K, Kato K. Int J Mol Sci 20 E2231 (2019)
  5. New insight into the dynamical system of αB-crystallin oligomers. Inoue R, Takata T, Fujii N, Ishii K, Uchiyama S, Sato N, Oba Y, Wood K, Kato K, Fujii N, Sugiyama M. Sci Rep 6 29208 (2016)
  6. Proteasome subunit α1 overexpression preferentially drives canonical proteasome biogenesis and enhances stress tolerance in yeast. Howell LA, Peterson AK, Tomko RJ. Sci Rep 9 12418 (2019)
  7. Overexpression of PSMA7 predicts poor prognosis in patients with gastric cancer. Xia S, Tang Q, Wang X, Zhang L, Jia L, Wu D, Xu P, Zhang X, Tang G, Yang T, Feng Z, Lu L. Oncol Lett 18 5341-5349 (2019)
  8. Assembly of proteasome subunits into non-canonical complexes in vivo. Hammack LJ, Kusmierczyk AR. Biochem Biophys Res Commun 482 164-169 (2017)
  9. SDS-induced oligomerization of Lys49-phospholipase A2 from snake venom. Matsui T, Kamata S, Ishii K, Maruno T, Ghanem N, Uchiyama S, Kato K, Suzuki A, Oda-Ueda N, Ogawa T, Tanaka Y. Sci Rep 9 2330 (2019)
  10. A Comprehensive Study of the Interaction between Peptidoglycan Fragments and the Extracellular Domain of Mycobacterium tuberculosis Ser/Thr Kinase PknB. Wang Q, Marchetti R, Prisic S, Ishii K, Arai Y, Ohta I, Inuki S, Uchiyama S, Silipo A, Molinaro A, Husson RN, Fukase K, Fujimoto Y. Chembiochem 18 2094-2098 (2017)
  11. RecA requires two molecules of Mg2+ ions for its optimal strand exchange activity in vitro. Kim R, Kanamaru S, Mikawa T, Prévost C, Ishii K, Ito K, Uchiyama S, Oda M, Iwasaki H, Kim SK, Takahashi M. Nucleic Acids Res 46 2548-2559 (2018)
  12. Expression, Functional Characterization, and Preliminary Crystallization of the Cochaperone Prefoldin from the Thermophilic Fungus Chaetomium thermophilum. Morita K, Yamamoto YY, Hori A, Obata T, Uno Y, Shinohara K, Noguchi K, Noi K, Ogura T, Ishii K, Kato K, Kato K, Kikumoto M, Arranz R, Valpuesta JM, Yohda M. Int J Mol Sci 19 E2452 (2018)
  13. Structural characterization of HypX responsible for CO biosynthesis in the maturation of NiFe-hydrogenase. Muraki N, Ishii K, Uchiyama S, Itoh SG, Okumura H, Aono S. Commun Biol 2 385 (2019)
  14. Supramolecular tholos-like architecture constituted by archaeal proteins without functional annotation. Yagi-Utsumi M, Sikdar A, Song C, Park J, Inoue R, Watanabe H, Burton-Smith RN, Kozai T, Suzuki T, Kodama A, Ishii K, Yagi H, Satoh T, Uchiyama S, Uchihashi T, Joo K, Lee J, Sugiyama M, Murata K, Kato K. Sci Rep 10 1540 (2020)


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