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Volumn 37, Issue 5, 2010, Pages 728-735

Structure of a Blm10 Complex Reveals Common Mechanisms for Proteasome Binding and Gate Opening

Author keywords

PROTEINS

Indexed keywords

PROTEASOME; PROTEIN BLM10; REGULATOR PROTEIN; UNCLASSIFIED DRUG;

EID: 77649243592     PISSN: 10972765     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.molcel.2010.02.002     Document Type: Article
Times cited : (131)

References (29)
  • 1
    • 0037248908 scopus 로고    scopus 로고
    • ATP hydrolysis by the proteasome regulatory complex PAN serves multiple functions in protein degradation
    • Benaroudj N., Zwickl P., Seemüller E., Baumeister W., and Goldberg A.L. ATP hydrolysis by the proteasome regulatory complex PAN serves multiple functions in protein degradation. Mol. Cell 11 (2003) 69-78
    • (2003) Mol. Cell , vol.11 , pp. 69-78
    • Benaroudj, N.1    Zwickl, P.2    Seemüller, E.3    Baumeister, W.4    Goldberg, A.L.5
  • 4
    • 6344289159 scopus 로고    scopus 로고
    • Expression of the expanded YFL007w ORF and assignment of the gene name BLM10
    • Doherty K., Pramanik A., Pride L., Lukose J., and Moore C.W. Expression of the expanded YFL007w ORF and assignment of the gene name BLM10. Yeast 21 (2004) 1021-1023
    • (2004) Yeast , vol.21 , pp. 1021-1023
    • Doherty, K.1    Pramanik, A.2    Pride, L.3    Lukose, J.4    Moore, C.W.5
  • 5
    • 0242522904 scopus 로고    scopus 로고
    • Blm3 is part of nascent proteasomes and is involved in a late stage of nuclear proteasome assembly
    • Fehlker M., Wendler P., Lehmann A., and Enenkel C. Blm3 is part of nascent proteasomes and is involved in a late stage of nuclear proteasome assembly. EMBO Rep. 4 (2003) 959-963
    • (2003) EMBO Rep. , vol.4 , pp. 959-963
    • Fehlker, M.1    Wendler, P.2    Lehmann, A.3    Enenkel, C.4
  • 6
    • 0043192299 scopus 로고    scopus 로고
    • The pore of activated 20S proteasomes has an ordered 7-fold symmetric conformation
    • Förster A., Whitby F.G., and Hill C.P. The pore of activated 20S proteasomes has an ordered 7-fold symmetric conformation. EMBO J. 22 (2003) 4356-4364
    • (2003) EMBO J. , vol.22 , pp. 4356-4364
    • Förster, A.1    Whitby, F.G.2    Hill, C.P.3
  • 7
    • 19444387760 scopus 로고    scopus 로고
    • The 1.9 A structure of a proteasome-11S activator complex and implications for proteasome-PAN/PA700 interactions
    • Förster A., Masters E.I., Whitby F.G., Robinson H., and Hill C.P. The 1.9 A structure of a proteasome-11S activator complex and implications for proteasome-PAN/PA700 interactions. Mol. Cell 18 (2005) 589-599
    • (2005) Mol. Cell , vol.18 , pp. 589-599
    • Förster, A.1    Masters, E.I.2    Whitby, F.G.3    Robinson, H.4    Hill, C.P.5
  • 8
    • 57649140340 scopus 로고    scopus 로고
    • Differential roles of the COOH termini of AAA subunits of PA700 (19 S regulator) in asymmetric assembly and activation of the 26 S proteasome
    • Gillette T.G., Kumar B., Thompson D., Slaughter C.A., and DeMartino G.N. Differential roles of the COOH termini of AAA subunits of PA700 (19 S regulator) in asymmetric assembly and activation of the 26 S proteasome. J. Biol. Chem. 283 (2008) 31813-31822
    • (2008) J. Biol. Chem. , vol.283 , pp. 31813-31822
    • Gillette, T.G.1    Kumar, B.2    Thompson, D.3    Slaughter, C.A.4    DeMartino, G.N.5
  • 9
    • 0036083396 scopus 로고    scopus 로고
    • The ubiquitin-proteasome proteolytic pathway: destruction for the sake of construction
    • Glickman M.H., and Ciechanover A. The ubiquitin-proteasome proteolytic pathway: destruction for the sake of construction. Physiol. Rev. 82 (2002) 373-428
    • (2002) Physiol. Rev. , vol.82 , pp. 373-428
    • Glickman, M.H.1    Ciechanover, A.2
  • 11
    • 33749265270 scopus 로고    scopus 로고
    • Structure of the Blm10-20 S proteasome complex by cryo-electron microscopy. Insights into the mechanism of activation of mature yeast proteasomes
    • Iwanczyk J., Sadre-Bazzaz K., Ferrell K., Kondrashkina E., Formosa T., Hill C.P., and Ortega J. Structure of the Blm10-20 S proteasome complex by cryo-electron microscopy. Insights into the mechanism of activation of mature yeast proteasomes. J. Mol. Biol. 363 (2006) 648-659
    • (2006) J. Mol. Biol. , vol.363 , pp. 648-659
    • Iwanczyk, J.1    Sadre-Bazzaz, K.2    Ferrell, K.3    Kondrashkina, E.4    Formosa, T.5    Hill, C.P.6    Ortega, J.7
  • 12
    • 1942489340 scopus 로고    scopus 로고
    • New HEAT-like repeat motifs in proteins regulating proteasome structure and function
    • Kajava A.V., Gorbea C., Ortega J., Rechsteiner M., and Steven A.C. New HEAT-like repeat motifs in proteins regulating proteasome structure and function. J. Struct. Biol. 146 (2004) 425-430
    • (2004) J. Struct. Biol. , vol.146 , pp. 425-430
    • Kajava, A.V.1    Gorbea, C.2    Ortega, J.3    Rechsteiner, M.4    Steven, A.C.5
  • 14
    • 57049135155 scopus 로고    scopus 로고
    • Blm10 binds to pre-activated proteasome core particles with open gate conformation
    • Lehmann A., Jechow K., and Enenkel C. Blm10 binds to pre-activated proteasome core particles with open gate conformation. EMBO Rep. 9 (2008) 1237-1243
    • (2008) EMBO Rep. , vol.9 , pp. 1237-1243
    • Lehmann, A.1    Jechow, K.2    Enenkel, C.3
  • 15
    • 0029042511 scopus 로고
    • Crystal structure of the 20S proteasome from the archaeon T. acidophilum at 3.4 A resolution
    • Löwe J., Stock D., Jap B., Zwickl P., Baumeister W., and Huber R. Crystal structure of the 20S proteasome from the archaeon T. acidophilum at 3.4 A resolution. Science 268 (1995) 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
  • 16
    • 70349127213 scopus 로고    scopus 로고
    • Inactivation of the 20S proteasome maturase, Ump1p, leads to the instability of mtDNA in Saccharomyces cerevisiae
    • Malc E., Dzierzbicki P., Kaniak A., Skoneczna A., and Ciesla Z. Inactivation of the 20S proteasome maturase, Ump1p, leads to the instability of mtDNA in Saccharomyces cerevisiae. Mutat. Res. 669 (2009) 95-103
    • (2009) Mutat. Res. , vol.669 , pp. 95-103
    • Malc, E.1    Dzierzbicki, P.2    Kaniak, A.3    Skoneczna, A.4    Ciesla, Z.5
  • 17
    • 36849024844 scopus 로고    scopus 로고
    • The C-terminal extension of the beta7 subunit and activator complexes stabilize nascent 20 S proteasomes and promote their maturation
    • Marques A.J., Glanemann C., Ramos P.C., and Dohmen R.J. The C-terminal extension of the beta7 subunit and activator complexes stabilize nascent 20 S proteasomes and promote their maturation. J. Biol. Chem. 282 (2007) 34869-34876
    • (2007) J. Biol. Chem. , vol.282 , pp. 34869-34876
    • Marques, A.J.1    Glanemann, C.2    Ramos, P.C.3    Dohmen, R.J.4
  • 18
    • 0038696703 scopus 로고
    • Tetrazolium overlay technique for population studies of respiration deficiency in yeast
    • Ogur M., St. John R., and Nagai S. Tetrazolium overlay technique for population studies of respiration deficiency in yeast. Science 125 (1957) 928-929
    • (1957) Science , vol.125 , pp. 928-929
    • Ogur, M.1    St. John, R.2    Nagai, S.3
  • 19
    • 42949096020 scopus 로고    scopus 로고
    • Mechanism of gate opening in the 20S proteasome by the proteasomal ATPases
    • Rabl J., Smith D.M., Yu Y., Chang S.C., Goldberg A.L., and Cheng Y. Mechanism of gate opening in the 20S proteasome by the proteasomal ATPases. Mol. Cell 30 (2008) 360-368
    • (2008) Mol. Cell , vol.30 , pp. 360-368
    • Rabl, J.1    Smith, D.M.2    Yu, Y.3    Chang, S.C.4    Goldberg, A.L.5    Cheng, Y.6
  • 20
    • 11844287006 scopus 로고    scopus 로고
    • Mobilizing the proteolytic machine: cell biological roles of proteasome activators and inhibitors
    • Rechsteiner M., and Hill C.P. Mobilizing the proteolytic machine: cell biological roles of proteasome activators and inhibitors. Trends Cell Biol. 15 (2005) 27-33
    • (2005) Trends Cell Biol. , vol.15 , pp. 27-33
    • Rechsteiner, M.1    Hill, C.P.2
  • 24
    • 34548274872 scopus 로고    scopus 로고
    • Docking of the proteasomal ATPases' carboxyl termini in the 20S proteasome's alpha ring opens the gate for substrate entry
    • Smith D.M., Chang S.C., Park S., Finley D., Cheng Y., and Goldberg A.L. Docking of the proteasomal ATPases' carboxyl termini in the 20S proteasome's alpha ring opens the gate for substrate entry. Mol. Cell 27 (2007) 731-744
    • (2007) Mol. Cell , vol.27 , pp. 731-744
    • Smith, D.M.1    Chang, S.C.2    Park, S.3    Finley, D.4    Cheng, Y.5    Goldberg, A.L.6
  • 27
    • 0036646488 scopus 로고    scopus 로고
    • PA200, a nuclear proteasome activator involved in DNA repair
    • Ustrell V., Hoffman L., Pratt G., and Rechsteiner M. PA200, a nuclear proteasome activator involved in DNA repair. EMBO J. 21 (2002) 3516-3525
    • (2002) EMBO J. , vol.21 , pp. 3516-3525
    • Ustrell, V.1    Hoffman, L.2    Pratt, G.3    Rechsteiner, M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.