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Volumn 290, Issue 11, 2015, Pages 6878-6889

Solution structure of yeast Rpn9: Insights into proteasome lid assembly

Author keywords

[No Author keywords available]

Indexed keywords

MEDICAL IMAGING;

EID: 84924891318     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M114.626762     Document Type: Article
Times cited : (11)

References (55)
  • 1
    • 0034296394 scopus 로고    scopus 로고
    • Basic medical research award: The ubiquitin system
    • Hershko, A., Ciechanover, A., and Varshavsky, A. (2000) Basic medical research award: the ubiquitin system. Nat. Med. 6, 1073-1081
    • (2000) Nat. Med. , vol.6 , pp. 1073-1081
    • Hershko, A.1    Ciechanover, A.2    Varshavsky, A.3
  • 2
    • 0036083396 scopus 로고    scopus 로고
    • The ubiquitin-proteasome proteolytic pathway: Destruction for the sake of construction
    • Glickman, M. H., and Ciechanover, A. (2002) The ubiquitin-proteasome proteolytic pathway: destruction for the sake of construction. Physiol. Rev. 82, 373-428
    • (2002) Physiol. Rev. , vol.82 , pp. 373-428
    • Glickman, M.H.1    Ciechanover, A.2
  • 3
    • 0346727127 scopus 로고    scopus 로고
    • Protein degradation and protection against misfolded or damaged proteins
    • Goldberg, A. L. (2003) Protein degradation and protection against misfolded or damaged proteins. Nature 426, 895-899
    • (2003) Nature , vol.426 , pp. 895-899
    • Goldberg, A.L.1
  • 7
    • 0029042511 scopus 로고
    • Crystal structure of the 20S proteasome from the archaeon T. acidophilum at 3.4 Å resolution
    • Löwe, J., Stock, D., Jap, B., Zwickl, P., Baumeister, W., and Huber, R. (1995) Crystal structure of the 20S proteasome from the archaeon T. acidophilum at 3.4 Å resolution. Science 268, 533-539
    • (1995) Science , vol.268 , pp. 533-539
    • Löwe, J.1    Stock, D.2    Jap, B.3    Zwickl, P.4    Baumeister, W.5    Huber, R.6
  • 8
    • 84883472009 scopus 로고    scopus 로고
    • Unveiling the long-held secrets of the 26S proteasome
    • Förster, F., Unverdorben, P., Sledź, P., and Baumeister, W. (2013) Unveiling the long-held secrets of the 26S proteasome. Structure 21, 1551-1562
    • (2013) Structure , vol.21 , pp. 1551-1562
    • Förster, F.1    Unverdorben, P.2    Sledź, P.3    Baumeister, W.4
  • 9
    • 0032483546 scopus 로고    scopus 로고
    • A subcomplex of the proteasome regulatory particle required for ubiquitin-conjugate degradation and related to the COP9-signalosome and eIF3
    • Glickman, M. H., Rubin, D. M., Coux, O., Wefes, I., Pfeifer, G., Cjeka, Z., Baumeister, W., Fried, V. A., and Finley, D. (1998) A subcomplex of the proteasome regulatory particle required for ubiquitin-conjugate degradation and related to the COP9-signalosome and eIF3. Cell 94, 615-623
    • (1998) Cell , vol.94 , pp. 615-623
    • Glickman, M.H.1    Rubin, D.M.2    Coux, O.3    Wefes, I.4    Pfeifer, G.5    Cjeka, Z.6    Baumeister, W.7    Fried, V.A.8    Finley, D.9
  • 11
    • 28444452611 scopus 로고    scopus 로고
    • ATP binding to PAN or the 26S ATPases causes association with the 20S proteasome, gate opening, and translocation of unfolded proteins
    • Smith, D. M., Kafri, G., Cheng, Y., Ng, D., Walz, T., and Goldberg, A. L. (2005) ATP binding to PAN or the 26S ATPases causes association with the 20S proteasome, gate opening, and translocation of unfolded proteins. Mol. Cell 20, 687-698
    • (2005) Mol. Cell , vol.20 , pp. 687-698
    • Smith, D.M.1    Kafri, G.2    Cheng, Y.3    Ng, D.4    Walz, T.5    Goldberg, A.L.6
  • 16
    • 84876909425 scopus 로고    scopus 로고
    • Structure of the 26S proteasome with ATP-γS bound provides insights into the mechanism of nucleotide-dependent substrate translocation
    • ͆ledź, P., Unverdorben, P., Beck, F., Pfeifer, G., Schweitzer, A., Förster, F., and Baumeister W. (2013) Structure of the 26S proteasome with ATP-γS bound provides insights into the mechanism of nucleotide-dependent substrate translocation. Proc. Natl. Acad. Sci. U.S.A. 110, 7264-7269
    • (2013) Proc. Natl. Acad. Sci. U.S.A. , vol.110 , pp. 7264-7269
    • ͆ledź, P.1    Unverdorben, P.2    Beck, F.3    Pfeifer, G.4    Schweitzer, A.5    Förster, F.6    Baumeister, W.7
  • 17
    • 84880157841 scopus 로고    scopus 로고
    • Conformational switching of the 26S proteasome enables substrate degradation
    • Matyskiela, M. E., Lander, G. C., and Martin, A. (2013) Conformational switching of the 26S proteasome enables substrate degradation. Nat. Struct. Mol. Biol. 20, 781-788
    • (2013) Nat. Struct. Mol. Biol. , vol.20 , pp. 781-788
    • Matyskiela, M.E.1    Lander, G.C.2    Martin, A.3
  • 19
    • 0037179694 scopus 로고    scopus 로고
    • A cryptic protease couples deubiquitination and degradation by the proteasome
    • Yao, T., and Cohen, R. E. (2002) A cryptic protease couples deubiquitination and degradation by the proteasome. Nature 419, 403-407
    • (2002) Nature , vol.419 , pp. 403-407
    • Yao, T.1    Cohen, R.E.2
  • 20
    • 0037131243 scopus 로고    scopus 로고
    • Role of Rpn11 metalloprotease in deubiquitination and degradation by the 26S proteasome
    • Verma, R., Aravind, L., Oania, R., McDonald, W. H., Yates, J. R., 3rd, Koonin, E. V., and Deshaies, R. J. (2002) Role of Rpn11 metalloprotease in deubiquitination and degradation by the 26S proteasome. Science 298, 611-615
    • (2002) Science , vol.298 , pp. 611-615
    • Verma, R.1    Aravind, L.2    Oania, R.3    McDonald, W.H.4    Yates, J.R.5    Koonin, E.V.6    Deshaies, R.J.7
  • 22
    • 84895868714 scopus 로고    scopus 로고
    • Structure of the Rpn11-Rpn8 dimer reveals mechanisms of substrate deubiquitination during proteasomal degradation
    • Worden, E. J., Padovani, C., and Martin, A. (2014) Structure of the Rpn11-Rpn8 dimer reveals mechanisms of substrate deubiquitination during proteasomal degradation. Nat. Struct. Mol. Biol. 21, 220-227
    • (2014) Nat. Struct. Mol. Biol. , vol.21 , pp. 220-227
    • Worden, E.J.1    Padovani, C.2    Martin, A.3
  • 23
    • 68349157358 scopus 로고    scopus 로고
    • PCI complexes: Beyond the proteasome, CSN, and eIF3 Troika
    • Pick, E., Hofmann, K., and Glickman, M. H. (2009) PCI complexes: beyond the proteasome, CSN, and eIF3 Troika. Mol. Cell 35, 260-264
    • (2009) Mol. Cell , vol.35 , pp. 260-264
    • Pick, E.1    Hofmann, K.2    Glickman, M.H.3
  • 24
    • 33747347236 scopus 로고    scopus 로고
    • Structural organization of the 19S proteasome lid: Insights from MS of intact complexes
    • Sharon, M., Taverner, T., Ambroggio, X. I., Deshaies, R. J., and Robinson, C. V. (2006) Structural organization of the 19S proteasome lid: insights from MS of intact complexes. PLoS Biol. 4, e267
    • (2006) PLoS Biol. , vol.4 , pp. e267
    • Sharon, M.1    Taverner, T.2    Ambroggio, X.I.3    Deshaies, R.J.4    Robinson, C.V.5
  • 26
    • 84883488318 scopus 로고    scopus 로고
    • Formation of an intricate helical bundle dictates the assembly of the 26S proteasome lid
    • Estrin, E., Lopez-Blanco, J. R., Chacón, P., and Martin, A. (2013) Formation of an intricate helical bundle dictates the assembly of the 26S proteasome lid. Structure 21, 1624-1635
    • (2013) Structure , vol.21 , pp. 1624-1635
    • Estrin, E.1    Lopez-Blanco, J.R.2    Chacón, P.3    Martin, A.4
  • 27
    • 84255162055 scopus 로고    scopus 로고
    • Incorporation of the Rpn12 subunit couples completion of proteasome regulatory particle lid assembly to lid-base joining
    • Tomko, R. J. Jr., and Hochstrasser, M. (2011) Incorporation of the Rpn12 subunit couples completion of proteasome regulatory particle lid assembly to lid-base joining. Mol. Cell 44, 907-917
    • (2011) Mol. Cell , vol.44 , pp. 907-917
    • Tomko, R.J.1    Hochstrasser, M.2
  • 28
    • 77953291910 scopus 로고    scopus 로고
    • Dissection of the assembly pathway of the proteasome lid in Saccharomyces cerevisiae
    • Fukunaga, K., Kudo, T., Toh-e, A., Tanaka, K., and Saeki, Y. (2010) Dissection of the assembly pathway of the proteasome lid in Saccharomyces cerevisiae. Biochem. Biophys. Res. Commun. 396, 1048-1053
    • (2010) Biochem. Biophys. Res. Commun. , vol.396 , pp. 1048-1053
    • Fukunaga, K.1    Kudo, T.2    Toh-e, A.3    Tanaka, K.4    Saeki, Y.5
  • 29
    • 0032823312 scopus 로고    scopus 로고
    • Rpn9 is required for efficient assembly of the yeast 26S proteasome
    • Takeuchi, J., Fujimuro, M., Yokosawa, H., Tanaka, K., and Toh-e, A. (1999) Rpn9 is required for efficient assembly of the yeast 26S proteasome. Mol. Cell. Biol. 19, 6575-6584
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 6575-6584
    • Takeuchi, J.1    Fujimuro, M.2    Yokosawa, H.3    Tanaka, K.4    Toh-e, A.5
  • 30
    • 33750064555 scopus 로고    scopus 로고
    • Down-regulation of the 26S proteasome subunit RPN9 inhibits viral systemic transport and alters plant vascular development
    • Jin, H., Li, S., and Villegas, A., Jr. (2006) Down-regulation of the 26S proteasome subunit RPN9 inhibits viral systemic transport and alters plant vascular development. Plant Physiol. 142, 651-661
    • (2006) Plant Physiol. , vol.142 , pp. 651-661
    • Jin, H.1    Li, S.2    Villegas, A.3
  • 31
    • 84879627193 scopus 로고    scopus 로고
    • 15N resonance assignments of Rpn9, a regulatory subunit of 26S proteasome from Saccharomyces cerevisiae
    • 15N resonance assignments of Rpn9, a regulatory subunit of 26S proteasome from Saccharomyces cerevisiae. Biomol. NMR Assign. 8, 307-311
    • (2014) Biomol. NMR Assign. , vol.8 , pp. 307-311
    • Wu, Y.1    Hu, Y.2    Jin, C.3
  • 32
    • 84883710495 scopus 로고    scopus 로고
    • 15N resonance assignments of theVWAdomain of Saccharomyces cerevisiae Rpn10, a regulatory subunit of 26S proteasome
    • 15N resonance assignments of theVWAdomain of Saccharomyces cerevisiae Rpn10, a regulatory subunit of 26S proteasome. Biomol. NMR Assign 8, 391-394
    • (2014) Biomol. NMR Assign , vol.8 , pp. 391-394
    • Wu, Y.1    Hu, Y.2    Jin, C.3
  • 33
    • 0034625121 scopus 로고    scopus 로고
    • Utilization of site-directed spin labeling and high-resolution heteronuclear nuclear magnetic resonance for global fold determination of large proteins with limited nuclear Overhauser effect data
    • Battiste, J. L., and Wagner, G. (2000) Utilization of site-directed spin labeling and high-resolution heteronuclear nuclear magnetic resonance for global fold determination of large proteins with limited nuclear Overhauser effect data. Biochemistry 39, 5355-5365
    • (2000) Biochemistry , vol.39 , pp. 5355-5365
    • Battiste, J.L.1    Wagner, G.2
  • 34
    • 0031760503 scopus 로고    scopus 로고
    • Tunable alignment of macromolecules by filamentous phage yields dipolar coupling interactions
    • Hansen, M. R., Mueller, L., and Pardi, A. (1998) Tunable alignment of macromolecules by filamentous phage yields dipolar coupling interactions. Nat. Struct. Biol. 5, 1065-1074
    • (1998) Nat. Struct. Biol. , vol.5 , pp. 1065-1074
    • Hansen, M.R.1    Mueller, L.2    Pardi, A.3
  • 35
    • 45149147257 scopus 로고    scopus 로고
    • Liquid crystalline phase of G-tetrad DNA for NMR study of detergent-solubilized proteins
    • Lorieau, J., Yao, L., and Bax, A. (2008) Liquid crystalline phase of G-tetrad DNA for NMR study of detergent-solubilized proteins. J. Am. Chem. Soc. 130, 7536-7537
    • (2008) J. Am. Chem. Soc. , vol.130 , pp. 7536-7537
    • Lorieau, J.1    Yao, L.2    Bax, A.3
  • 36
    • 0032042263 scopus 로고    scopus 로고
    • Measurement of J and dipolar couplings from simplified two-dimensional NMR spectra
    • Ottiger, M., Delaglio, F., and Bax, A. (1998) Measurement of J and dipolar couplings from simplified two-dimensional NMR spectra. J. Magn. Reson. 131, 373-378
    • (1998) J. Magn. Reson. , vol.131 , pp. 373-378
    • Ottiger, M.1    Delaglio, F.2    Bax, A.3
  • 37
    • 0031576336 scopus 로고    scopus 로고
    • Torsion angle dynamics for NMR structure calculation with the new program DYANA
    • Güntert, P., Mumenthaler, C., and Wüthrich, K. (1997) Torsion angle dynamics for NMR structure calculation with the new program DYANA. J. Mol. Biol. 273, 283-298
    • (1997) J. Mol. Biol. , vol.273 , pp. 283-298
    • Güntert, P.1    Mumenthaler, C.2    Wüthrich, K.3
  • 38
    • 0036308102 scopus 로고    scopus 로고
    • Protein NMR structure determination with automated NOE assignment using the new software CANDID and the torsion angle dynamics algorithm DYANA
    • Herrmann, T., Güntert, P., and Wüthrich, K. (2002) Protein NMR structure determination with automated NOE assignment using the new software CANDID and the torsion angle dynamics algorithm DYANA. J. Mol. Biol. 319, 209-227
    • (2002) J. Mol. Biol. , vol.319 , pp. 209-227
    • Herrmann, T.1    Güntert, P.2    Wüthrich, K.3
  • 39
    • 0033003335 scopus 로고    scopus 로고
    • Protein backbone angle restraints from searching a database for chemical shift and sequence homology
    • Cornilescu, G., Delaglio, F., and Bax, A. (1999) Protein backbone angle restraints from searching a database for chemical shift and sequence homology. J. Biomol. NMR 13, 289-302
    • (1999) J. Biomol. NMR , vol.13 , pp. 289-302
    • Cornilescu, G.1    Delaglio, F.2    Bax, A.3
  • 40
    • 0035029325 scopus 로고    scopus 로고
    • SANE (Structure Assisted NOE Evaluation): An automated model-based approach for NOE assignment
    • Duggan, B. M., Legge, G. B., Dyson, H. J., and Wright, P. E. (2001) SANE (Structure Assisted NOE Evaluation): an automated model-based approach for NOE assignment. J. Biomol. NMR 19, 321-329
    • (2001) J. Biomol. NMR , vol.19 , pp. 321-329
    • Duggan, B.M.1    Legge, G.B.2    Dyson, H.J.3    Wright, P.E.4
  • 42
    • 0032780181 scopus 로고    scopus 로고
    • Situs: A package for docking crystal structures into low-resolution maps from electron microscopy
    • Wriggers, W., Milligan, R. A., McCammon, J. A. (1999) Situs: a package for docking crystal structures into low-resolution maps from electron microscopy. J. Struct. Biol. 125, 185-195
    • (1999) J. Struct. Biol. , vol.125 , pp. 185-195
    • Wriggers, W.1    Milligan, R.A.2    McCammon, J.A.3
  • 44
    • 42949089487 scopus 로고    scopus 로고
    • Flexible fitting of atomic structures into electron microscopy maps using molecular dynamics
    • Trabuco, L. G., Villa, E., Mitra, K., Frank, J., and Schulten, K. (2008) Flexible fitting of atomic structures into electron microscopy maps using molecular dynamics. Structure 16, 673-683
    • (2008) Structure , vol.16 , pp. 673-683
    • Trabuco, L.G.1    Villa, E.2    Mitra, K.3    Frank, J.4    Schulten, K.5
  • 45
    • 33845345287 scopus 로고    scopus 로고
    • Visualizing density maps with UCSF Chimera
    • Goddard, T. D., Huang, C. C., and Ferrin, T. E. (2007) Visualizing density maps with UCSF Chimera. J. Struct. Biol. 157, 281-287
    • (2007) J. Struct. Biol. , vol.157 , pp. 281-287
    • Goddard, T.D.1    Huang, C.C.2    Ferrin, T.E.3
  • 46
    • 84881115632 scopus 로고    scopus 로고
    • Tandem-repeat proteins: Regularity plus modularity equals design-ability
    • Javadi, Y., and Itzhaki, L. S. (2013) Tandem-repeat proteins: regularity plus modularity equals design-ability. Curr. Opin. Struct. Biol. 23, 622-631
    • (2013) Curr. Opin. Struct. Biol. , vol.23 , pp. 622-631
    • Javadi, Y.1    Itzhaki, L.S.2
  • 49
    • 57749097584 scopus 로고    scopus 로고
    • The Arabidopsis COP9 signalosome subunit 7 is a model PCI domain protein with subdomains involved in COP9 signalosome assembly
    • Dessau, M., Halimi, Y., Erez, T., Chomsky-Hecht, O., Chamovitz, D. A., and Hirsch, J. A. (2008) The Arabidopsis COP9 signalosome subunit 7 is a model PCI domain protein with subdomains involved in COP9 signalosome assembly. Plant Cell 20, 2815-2834
    • (2008) Plant Cell , vol.20 , pp. 2815-2834
    • Dessau, M.1    Halimi, Y.2    Erez, T.3    Chomsky-Hecht, O.4    Chamovitz, D.A.5    Hirsch, J.A.6
  • 50
    • 4544304063 scopus 로고    scopus 로고
    • Crystal structure of human eIF3k, the first structure of eIF3 subunits
    • Wei, Z., Zhang, P., Zhou, Z., Cheng, Z., Wan, M., and Gong, W. (2004) Crystal structure of human eIF3k, the first structure of eIF3 subunits. J. Biol. Chem. 279, 34983-34990
    • (2004) J. Biol. Chem. , vol.279 , pp. 34983-34990
    • Wei, Z.1    Zhang, P.2    Zhou, Z.3    Cheng, Z.4    Wan, M.5    Gong, W.6
  • 51
    • 66549119395 scopus 로고    scopus 로고
    • Advances and pitfalls of protein structural alignment
    • Hasegawa, H., and Holm, L. (2009) Advances and pitfalls of protein structural alignment. Curr. Opin. Struct. Biol. 19, 341-348
    • (2009) Curr. Opin. Struct. Biol. , vol.19 , pp. 341-348
    • Hasegawa, H.1    Holm, L.2
  • 52
    • 84873652229 scopus 로고    scopus 로고
    • Duplication and familial promiscuity within the proteasome lid and COP9 signalosome kin complexes
    • Serino, G., and Pick, E. (2013) Duplication and familial promiscuity within the proteasome lid and COP9 signalosome kin complexes. Plant Sci. 203, 89-97
    • (2013) Plant Sci. , vol.203 , pp. 89-97
    • Serino, G.1    Pick, E.2
  • 53
    • 0034884233 scopus 로고    scopus 로고
    • A novel interactive tool for rigid-body modeling of multi-domain macromolecules using residual dipolar couplings
    • Dosset, P., Hus, J. C., Marion, D., and Blackledge, M. (2001) A novel interactive tool for rigid-body modeling of multi-domain macromolecules using residual dipolar couplings. J. Biomol NMR 20, 223-231
    • (2001) J. Biomol NMR , vol.20 , pp. 223-231
    • Dosset, P.1    Hus, J.C.2    Marion, D.3    Blackledge, M.4
  • 54
    • 0033551495 scopus 로고    scopus 로고
    • Domain orientation and dynamics in multidomain proteins from residual dipolar couplings
    • Fischer, M. W., Losonczi, J. A., Weaver, J. L., and Prestegard, J. H. (1999) Domain orientation and dynamics in multidomain proteins from residual dipolar couplings. Biochemistry 38, 9013-9022
    • (1999) Biochemistry , vol.38 , pp. 9013-9022
    • Fischer, M.W.1    Losonczi, J.A.2    Weaver, J.L.3    Prestegard, J.H.4
  • 55
    • 2542445427 scopus 로고    scopus 로고
    • ConSurf: Identification of functional regions in proteins by surface-mapping of phylogenetic information
    • Glaser, F., Pupko, T., Paz, I., Bell, R. E., Bechor-Shental, D., Martz, E., and Ben-Tal, N. (2003) ConSurf: identification of functional regions in proteins by surface-mapping of phylogenetic information. Bioinformatics 19, 163-164
    • (2003) Bioinformatics , vol.19 , pp. 163-164
    • Glaser, F.1    Pupko, T.2    Paz, I.3    Bell, R.E.4    Bechor-Shental, D.5    Martz, E.6    Ben-Tal, N.7


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