메뉴 건너뛰기




Volumn 35, Issue 1, 2015, Pages 141-152

N-terminal α7 deletion of the proteasome 20S core particle substitutes for yeast PI31 function

Author keywords

[No Author keywords available]

Indexed keywords

CORE PROTEIN; FUB1 PROTEIN; FUNGAL PROTEIN; PBA3 PROTEIN; PBA4 PROTEIN; PI31 PROTEIN; PROTEASOME; PROTEASOME 20S CORE PARTICLE; UNCLASSIFIED DRUG; FUB1 PROTEIN, S CEREVISIAE; GLYCEROL; PROTEIN BINDING; SACCHAROMYCES CEREVISIAE PROTEIN;

EID: 84920055188     PISSN: 02707306     EISSN: 10985549     Source Type: Journal    
DOI: 10.1128/MCB.00582-14     Document Type: Article
Times cited : (12)

References (47)
  • 1
    • 59249084491 scopus 로고    scopus 로고
    • The proteasome: overview of structure and functions
    • Tanaka K. 2009. The proteasome: overview of structure and functions. Proc Jpn Acad Ser B Phys Biol Sci 85:12-36. http://dx.doi.org/10.2183/pjab.85.12.
    • (2009) Proc Jpn Acad Ser B Phys Biol Sci , vol.85 , pp. 12-36
    • Tanaka, K.1
  • 3
    • 19444387760 scopus 로고    scopus 로고
    • The 1.9 A structure of a proteasome-11S activator complex and implications for proteasome-PAN/PA700 interactions
    • Forster A, Masters EI, Whitby FG, Robinson H, Hill CP. 2005. The 1.9 A structure of a proteasome-11S activator complex and implications for proteasome-PAN/PA700 interactions. Mol Cell 18:589-599. http://dx.doi.org/10.1016/j.molcel.2005.04.016.
    • (2005) Mol Cell , vol.18 , pp. 589-599
    • Forster, A.1    Masters, E.I.2    Whitby, F.G.3    Robinson, H.4    Hill, C.P.5
  • 7
    • 76349089770 scopus 로고    scopus 로고
    • Interactions of PAN=s C-termini with archaeal 20S proteasome and implications for the eukaryotic proteasome-ATPase interactions
    • Yu Y, Smith DM, Kim HM, Rodriguez V, Goldberg AL, Cheng Y. 2010. Interactions of PAN=s C-termini with archaeal 20S proteasome and implications for the eukaryotic proteasome-ATPase interactions. EMBO J 29:692-702. http://dx.doi.org/10.1038/emboj.2009.382.
    • (2010) EMBO J , vol.29 , pp. 692-702
    • Yu, Y.1    Smith, D.M.2    Kim, H.M.3    Rodriguez, V.4    Goldberg, A.L.5    Cheng, Y.6
  • 8
    • 77954314106 scopus 로고    scopus 로고
    • Assembly, structure, and function of the 26S proteasome
    • Bedford L, Paine S, Sheppard PW, Mayer RJ, Roelofs J. 2010. Assembly, structure, and function of the 26S proteasome. Trends Cell Biol. 20:391-401. http://dx.doi.org/10.1016/j.tcb.2010.03.007.
    • (2010) Trends Cell Biol. , vol.20 , pp. 391-401
    • Bedford, L.1    Paine, S.2    Sheppard, P.W.3    Mayer, R.J.4    Roelofs, J.5
  • 9
    • 54049107641 scopus 로고    scopus 로고
    • Some assembly required: dedicated chaperones in eukaryotic proteasome biogenesis
    • Kusmierczyk AR, Hochstrasser M. 2008. Some assembly required: dedicated chaperones in eukaryotic proteasome biogenesis. Biol Chem 389: 1143-1151. http://dx.doi.org/10.1515/BC.2008.130.
    • (2008) Biol Chem , vol.389 , pp. 1143-1151
    • Kusmierczyk, A.R.1    Hochstrasser, M.2
  • 10
    • 50849123778 scopus 로고    scopus 로고
    • PACemakers of proteasome core particle assembly
    • Ramos PC, Dohmen RJ. 2008. PACemakers of proteasome core particle assembly. Structure 16:1296-1304. http://dx.doi.org/10.1016/j.str.2008.07.001.
    • (2008) Structure , vol.16 , pp. 1296-1304
    • Ramos, P.C.1    Dohmen, R.J.2
  • 11
    • 53849136910 scopus 로고    scopus 로고
    • Chaperone-driven proteasome assembly
    • Rosenzweig R, Glickman MH. 2008. Chaperone-driven proteasome assembly. Biochem Soc Trans 36:807-812. http://dx.doi.org/10.1042/BST0360807.
    • (2008) Biochem Soc Trans , vol.36 , pp. 807-812
    • Rosenzweig, R.1    Glickman, M.H.2
  • 12
    • 58849093135 scopus 로고    scopus 로고
    • Molecular mechanisms of proteasome assembly
    • Murata S, Yashiroda H, Tanaka K. 2009. Molecular mechanisms of proteasome assembly. Nat Rev Mol Cell Biol 10:104-115. http://dx.doi.org/10.1038/nrm2630.
    • (2009) Nat Rev Mol Cell Biol , vol.10 , pp. 104-115
    • Murata, S.1    Yashiroda, H.2    Tanaka, K.3
  • 13
    • 76449099938 scopus 로고    scopus 로고
    • Chaperone-assisted assembly of the proteasome core particle
    • Matias AC, Ramos PC, Dohmen RJ. 2010. Chaperone-assisted assembly of the proteasome core particle. Biochem Soc Trans 38:29-33. http://dx.doi.org/10.1042/BST0380029.
    • (2010) Biochem Soc Trans , vol.38 , pp. 29-33
    • Matias, A.C.1    Ramos, P.C.2    Dohmen, R.J.3
  • 16
    • 40949117574 scopus 로고    scopus 로고
    • A multimeric assembly factor controls the formation of alternative 20S proteasomes
    • Kusmierczyk AR, Kunjappu MJ, Funakoshi M, Hochstrasser M. 2008. A multimeric assembly factor controls the formation of alternative 20S proteasomes. Nat Struct Mol Biol 15:237-244. http://dx.doi.org/10.1038/nsmb.1389.
    • (2008) Nat Struct Mol Biol , vol.15 , pp. 237-244
    • Kusmierczyk, A.R.1    Kunjappu, M.J.2    Funakoshi, M.3    Hochstrasser, M.4
  • 18
    • 41549109801 scopus 로고    scopus 로고
    • A genetic screen for Saccharomyces cerevisiae mutants affecting proteasome function, using a ubiquitin-independent substrate
    • Hoyt MA, McDonough S, Pimpl SA, Scheel H, Hofmann K, Coffino P. 2008. A genetic screen for Saccharomyces cerevisiae mutants affecting proteasome function, using a ubiquitin-independent substrate. Yeast 25: 199-217. http://dx.doi.org/10.1002/yea.1579.
    • (2008) Yeast , vol.25 , pp. 199-217
    • Hoyt, M.A.1    McDonough, S.2    Pimpl, S.A.3    Scheel, H.4    Hofmann, K.5    Coffino, P.6
  • 19
    • 34547838178 scopus 로고    scopus 로고
    • 20S proteasome assembly is orchestrated by two distinct pairs of chaperones in yeast and in mammals
    • Le Tallec B, Barrault MB, Courbeyrette R, Guerois R, Marsolier- Kergoat MC, Peyroche A. 2007. 20S proteasome assembly is orchestrated by two distinct pairs of chaperones in yeast and in mammals. Mol Cell 27:660-674. http://dx.doi.org/10.1016/j.molcel.2007.06.025.
    • (2007) Mol Cell , vol.27 , pp. 660-674
    • Le Tallec, B.1    Barrault, M.B.2    Courbeyrette, R.3    Guerois, R.4    Marsolier-Kergoat, M.C.5    Peyroche, A.6
  • 20
    • 0026506729 scopus 로고
    • Purification and characterization of a protein inhibitor of the 20S proteasome (macropain)
    • Chu-Ping M, Slaughter CA, DeMartino GN. 1992. Purification and characterization of a protein inhibitor of the 20S proteasome (macropain). Biochim Biophys Acta 1119:303-311. http://dx.doi.org/10.1016/0167-4838(92)90218-3.
    • (1992) Biochim Biophys Acta , vol.1119 , pp. 303-311
    • Chu-Ping, M.1    Slaughter, C.A.2    DeMartino, G.N.3
  • 21
    • 0034674655 scopus 로고    scopus 로고
    • cDNA cloning, expression, and functional characterization of PI31, a proline-rich inhibitor of the proteasome
    • McCutchen-Maloney SL, Matsuda K, Shimbara N, Binns DD, Tanaka K, Slaughter CA, DeMartino GN. 2000. cDNA cloning, expression, and functional characterization of PI31, a proline-rich inhibitor of the proteasome. J Biol Chem 275:18557-18565. http://dx.doi.org/10.1074/jbc. M001697200.
    • (2000) J Biol Chem , vol.275 , pp. 18557-18565
    • McCutchen-Maloney, S.L.1    Matsuda, K.2    Shimbara, N.3    Binns, D.D.4    Tanaka, K.5    Slaughter, C.A.6    DeMartino, G.N.7
  • 22
    • 0032828077 scopus 로고    scopus 로고
    • The proteasome inhibitor PI31 competes with PA28 for binding to 20S proteasomes
    • Zaiss DM, Standera S, Holzhutter H, Kloetzel P, Sijts AJ. 1999. The proteasome inhibitor PI31 competes with PA28 for binding to 20S proteasomes. FEBS Lett 457:333-338. http://dx.doi.org/10.1016/S0014-5793(99)01072-8.
    • (1999) FEBS Lett , vol.457 , pp. 333-338
    • Zaiss, D.M.1    Standera, S.2    Holzhutter, H.3    Kloetzel, P.4    Sijts, A.J.5
  • 23
    • 0037195136 scopus 로고    scopus 로고
    • PI31 is a modulator of proteasome formation and antigen processing
    • Zaiss DM, Standera S, Kloetzel PM, Sijts AJ. 2002. PI31 is a modulator of proteasome formation and antigen processing. Proc Natl Acad SciUSA 99:14344-14349. http://dx.doi.org/10.1073/pnas.212257299.
    • (2002) Proc Natl Acad SciUSA , vol.99 , pp. 14344-14349
    • Zaiss, D.M.1    Standera, S.2    Kloetzel, P.M.3    Sijts, A.J.4
  • 24
    • 79955544968 scopus 로고    scopus 로고
    • A conserved F box regulatory complex controls proteasome activity in Drosophila
    • Bader M, Benjamin S, Wapinski OL, Smith DM, Goldberg AL, Steller H. 2011. A conserved F box regulatory complex controls proteasome activity in Drosophila. Cell 145:371-382. http://dx.doi.org/10.1016/j.cell.2011.03.021.
    • (2011) Cell , vol.145 , pp. 371-382
    • Bader, M.1    Benjamin, S.2    Wapinski, O.L.3    Smith, D.M.4    Goldberg, A.L.5    Steller, H.6
  • 25
    • 84876935501 scopus 로고    scopus 로고
    • Proteasome regulation by ADP-ribosylation
    • Cho-Park PF, Steller H. 2013. Proteasome regulation by ADP-ribosylation. Cell 153:614-627. http://dx.doi.org/10.1016/j.cell.2013.03.040.
    • (2013) Cell , vol.153 , pp. 614-627
    • Cho-Park, P.F.1    Steller, H.2
  • 26
    • 84903475943 scopus 로고    scopus 로고
    • Molecular and cellular roles of PI31 (PSMF1) protein in regulation of proteasome function
    • Li X, Thompson D, Kumar B, DeMartino GN. 2014. Molecular and cellular roles of PI31 (PSMF1) protein in regulation of proteasome function. J Biol Chem 289:17392-17405. http://dx.doi.org/10.1074/jbc. M114.561183.
    • (2014) J Biol Chem , vol.289 , pp. 17392-17405
    • Li, X.1    Thompson, D.2    Kumar, B.3    DeMartino, G.N.4
  • 30
    • 28844484999 scopus 로고    scopus 로고
    • Preparation of ubiquitinated substrates by the PY motif-insertion method for monitoring 26S proteasome activity
    • Saeki Y, Isono E, Toh EA. 2005. Preparation of ubiquitinated substrates by the PY motif-insertion method for monitoring 26S proteasome activity. Methods Enzymol 399:215-227. http://dx.doi.org/10.1016/S0076-6879(05)99014-9.
    • (2005) Methods Enzymol , vol.399 , pp. 215-227
    • Saeki, Y.1    Isono, E.2    Toh, E.A.3
  • 31
    • 77956838037 scopus 로고    scopus 로고
    • Upregulation of the PRB1 gene in the Saccharomyces cerevisiae rim101Delta mutant produces proteolytic artefacts that differentially affect some proteins
    • Perez J, Gomez A, Roncero C. 2010. Upregulation of the PRB1 gene in the Saccharomyces cerevisiae rim101Delta mutant produces proteolytic artefacts that differentially affect some proteins. Yeast 27:575-581. http://dx.doi.org/10.1002/yea.1776.
    • (2010) Yeast , vol.27 , pp. 575-581
    • Perez, J.1    Gomez, A.2    Roncero, C.3
  • 32
    • 27644576445 scopus 로고    scopus 로고
    • Characterization of the proteasome using native gel electrophoresis
    • Elsasser S, Schmidt M, Finley D. 2005. Characterization of the proteasome using native gel electrophoresis. Methods Enzymol 398:353-363. http://dx.doi.org/10.1016/S0076-6879(05)98029-4.
    • (2005) Methods Enzymol , vol.398 , pp. 353-363
    • Elsasser, S.1    Schmidt, M.2    Finley, D.3
  • 33
    • 0034761941 scopus 로고    scopus 로고
    • Initial process of polyglutamine aggregate formation in vivo
    • Kimura Y, Koitabashi S, Kakizuka A, Fujita T. 2001. Initial process of polyglutamine aggregate formation in vivo. Genes Cells 6:887-897. http://dx.doi.org/10.1046/j.1365-2443.2001.00472.x.
    • (2001) Genes Cells , vol.6 , pp. 887-897
    • Kimura, Y.1    Koitabashi, S.2    Kakizuka, A.3    Fujita, T.4
  • 34
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski Z, Minor W. 1997. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol 276:307-326. http://dx.doi.org/10.1016/S0076-6879(97)76066-X.
    • (1997) Methods Enzymol , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 35
  • 36
    • 13244281317 scopus 로고    scopus 로고
    • Coot: model-building tools for molecular graphics
    • Emsley P, Cowtan K. 2004. Coot: model-building tools for molecular graphics. Acta Crystallogr D Biol Crystallogr 60:2126-2132. http://dx.doi.org/10.1107/S0907444904019158.
    • (2004) Acta Crystallogr D Biol Crystallogr , vol.60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 37
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolecular structures by the maximum-likelihood method
    • Murshudov GN, Vagin AA, Dodson EJ. 1997. Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallogr D Biol Crystallogr 53:240-255. http://dx.doi.org/10.1107/S0907444996012255.
    • (1997) Acta Crystallogr D Biol Crystallogr , vol.53 , pp. 240-255
    • Murshudov, G.N.1    Vagin, A.A.2    Dodson, E.J.3
  • 40
    • 52049116958 scopus 로고    scopus 로고
    • Structure of a conserved dimerization domain within the F-box protein Fbxo7 and the PI31 proteasome inhibitor
    • Kirk R, Laman H, Knowles PP, Murray-Rust J, Lomonosov M, Meziane EK, McDonald NQ. 2008. Structure of a conserved dimerization domain within the F-box protein Fbxo7 and the PI31 proteasome inhibitor. J Biol Chem 283:22325-22335. http://dx.doi.org/10.1074/jbc. M709900200.
    • (2008) J Biol Chem , vol.283 , pp. 22325-22335
    • Kirk, R.1    Laman, H.2    Knowles, P.P.3    Murray-Rust, J.4    Lomonosov, M.5    Meziane, E.K.6    McDonald, N.Q.7
  • 41
    • 1442264792 scopus 로고    scopus 로고
    • Plasticity in eucaryotic 20S proteasome ring assembly revealed by a subunit deletion in yeast
    • Velichutina I, Connerly PL, Arendt CS, Li X, Hochstrasser M. 2004. Plasticity in eucaryotic 20S proteasome ring assembly revealed by a subunit deletion in yeast. EMBO J 23:500-510. http://dx.doi.org/10.1038/sj.emboj.7600059.
    • (2004) EMBO J , vol.23 , pp. 500-510
    • Velichutina, I.1    Connerly, P.L.2    Arendt, C.S.3    Li, X.4    Hochstrasser, M.5
  • 42
    • 0038686574 scopus 로고    scopus 로고
    • Proteasome disassembly and downregulation is correlated with viability during stationary phase
    • Bajorek M, Finley D, Glickman MH. 2003. Proteasome disassembly and downregulation is correlated with viability during stationary phase. Curr Biol 13:1140-1144. http://dx.doi.org/10.1016/S0960-9822(03)00417-2.
    • (2003) Curr Biol , vol.13 , pp. 1140-1144
    • Bajorek, M.1    Finley, D.2    Glickman, M.H.3
  • 43
    • 0037449572 scopus 로고    scopus 로고
    • Endoproteolytic activity of the proteasome
    • Liu CW, Corboy MJ, DeMartino GN, Thomas PJ. 2003. Endoproteolytic activity of the proteasome. Science 299:408-411. http://dx.doi.org/10.1126/science.1079293.
    • (2003) Science , vol.299 , pp. 408-411
    • Liu, C.W.1    Corboy, M.J.2    DeMartino, G.N.3    Thomas, P.J.4
  • 44
    • 79959888485 scopus 로고    scopus 로고
    • Exposed hydrophobicity is a key determinant of nuclear quality control degradation
    • Fredrickson EK, Rosenbaum JC, Locke MN, Milac TI, Gardner RG. 2011. Exposed hydrophobicity is a key determinant of nuclear quality control degradation. Mol Biol Cell 22:2384-2395. http://dx.doi.org/10.1091/mbc. E11-03-0256.
    • (2011) Mol Biol Cell , vol.22 , pp. 2384-2395
    • Fredrickson, E.K.1    Rosenbaum, J.C.2    Locke, M.N.3    Milac, T.I.4    Gardner, R.G.5
  • 45
    • 0024669291 scopus 로고
    • A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae
    • Sikorski RS, Hieter P. 1989. A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae. Genetics 122:19-27.
    • (1989) Genetics , vol.122 , pp. 19-27
    • Sikorski, R.S.1    Hieter, P.2
  • 46
    • 10244223979 scopus 로고    scopus 로고
    • Hub1 is an essential ubiquitin-like protein without functioning as a typical modifier in fission yeast
    • Yashiroda H, Tanaka K. 2004. Hub1 is an essential ubiquitin-like protein without functioning as a typical modifier in fission yeast. Genes Cells 9:1189-1197. http://dx.doi.org/10.1111/j.1365-2443.2004.00807.x.
    • (2004) Genes Cells , vol.9 , pp. 1189-1197
    • Yashiroda, H.1    Tanaka, K.2
  • 47
    • 0026687986 scopus 로고
    • RHO gene products, putative small GTP-binding proteins, are important for activation of the CAL1/CDC43 gene product, a protein geranylgeranyltransferase in Saccharomyces cerevisiae
    • Qadota H, Ishii I, Fujiyama A, Ohya Y, Anraku Y. 1992. RHO gene products, putative small GTP-binding proteins, are important for activation of the CAL1/CDC43 gene product, a protein geranylgeranyltransferase in Saccharomyces cerevisiae. Yeast 8:735-741. http://dx.doi.org/10.1002/yea.320080906.
    • (1992) Yeast , vol.8 , pp. 735-741
    • Qadota, H.1    Ishii, I.2    Fujiyama, A.3    Ohya, Y.4    Anraku, Y.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.