메뉴 건너뛰기




Volumn 43, Issue 6, 2015, Pages 3358-3372

Crystal structures of the Gon7/Pcc1 and Bud32/Cgi121 complexes provide a model for the complete yeast KEOPS complex

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE DIPHOSPHATE; ARCHAEAL PROTEIN; BUD32 PROTEIN; CGI121 PROTEIN; CYCLIC AMP DEPENDENT PROTEIN KINASE; DIMER; FUNGAL PROTEIN; GON7 PROTEIN; HETERODIMER; KAE1 PROTEIN; KEOPS PROTEIN COMPLEX; PCC1 PROTEIN; TRANSFER RNA; UNCLASSIFIED DRUG; BUD32 PROTEIN, S CEREVISIAE; KEOPS COMPLEX, S CEREVISIAE; MULTIPROTEIN COMPLEX; PCC1 PROTEIN, S CEREVISIAE; PROTEIN SERINE THREONINE KINASE; RECOMBINANT PROTEIN; SACCHAROMYCES CEREVISIAE PROTEIN; TRANSCRIPTION FACTOR;

EID: 84941942173     PISSN: 03051048     EISSN: 13624962     Source Type: Journal    
DOI: 10.1093/nar/gkv155     Document Type: Article
Times cited : (34)

References (58)
  • 1
    • 0014503343 scopus 로고
    • The primary structure of isoleucine transfer ribonucleic acid from Torulopsis utilis. Complete digestion with ribonucleases and construction of model of its secondary structure
    • Takemura,S., Murakami,M. and Miyazaki,M. (1969) The primary structure of isoleucine transfer ribonucleic acid from Torulopsis utilis. Complete digestion with ribonucleases and construction of model of its secondary structure. J. Biochem., 65, 553-566.
    • (1969) J. Biochem. , vol.65 , pp. 553-566
    • Takemura, S.1    Murakami, M.2    Miyazaki, M.3
  • 2
    • 0016261534 scopus 로고
    • Conformation and possible role of hypermodified nucleosides adjacent to 3′-end of anticodon in tRNA: N-(purin-6-ylcarbamoyl)-L-threonine riboside
    • Parthasarathy,R., Ohrt,J.M. and Chheda,G.B. (1974) Conformation and possible role of hypermodified nucleosides adjacent to 3′-end of anticodon in tRNA: N-(purin-6-ylcarbamoyl)-L-threonine riboside. Biochem. Biophys. Res. Commun., 60, 211-218.
    • (1974) Biochem. Biophys. Res. Commun. , vol.60 , pp. 211-218
    • Parthasarathy, R.1    Ohrt, J.M.2    Chheda, G.B.3
  • 6
    • 79952280840 scopus 로고    scopus 로고
    • The highly conserved KEOPS/EKC complex is essential for a universal tRNA modification, t6A
    • Srinivasan,M., Mehta,P., Yu,Y., Prugar,E., Koonin,E.V., Karzai,A.W. and Sternglanz,R. (2011) The highly conserved KEOPS/EKC complex is essential for a universal tRNA modification, t6A. EMBO J., 30, 873-881.
    • (2011) EMBO J. , vol.30 , pp. 873-881
    • Srinivasan, M.1    Mehta, P.2    Yu, Y.3    Prugar, E.4    Koonin, E.V.5    Karzai, A.W.6    Sternglanz, R.7
  • 9
    • 84890067053 scopus 로고    scopus 로고
    • Functional assignment of KEOPS/EKC complex subunits in the biosynthesis of the universal t6A tRNA modification
    • Perrochia,L., Guetta,D., Hecker,A., Forterre,P. and Basta,T. (2013) Functional assignment of KEOPS/EKC complex subunits in the biosynthesis of the universal t6A tRNA modification. Nucleic Acids Res., 41, 9484-9499.
    • (2013) Nucleic Acids Res. , vol.41 , pp. 9484-9499
    • Perrochia, L.1    Guetta, D.2    Hecker, A.3    Forterre, P.4    Basta, T.5
  • 10
    • 84859994582 scopus 로고    scopus 로고
    • The biosynthesis of threonylcarbamoyl adenosine (t6A), a universal tRNA nucleoside
    • Deutsch,C., El Yacoubi,B., de Crecy-Lagard,V. and Iwata-Reuyl,D. (2012) The biosynthesis of threonylcarbamoyl adenosine (t6A), a universal tRNA nucleoside. J. Biol. Chem., 287, 13666-13673.
    • (2012) J. Biol. Chem. , vol.287 , pp. 13666-13673
    • Deutsch, C.1    El Yacoubi, B.2    De Crecy-Lagard, V.3    Iwata-Reuyl, D.4
  • 11
    • 84936743574 scopus 로고    scopus 로고
    • The ATP-mediated formation of the YgjD-YeaZ-YjeE complex is required for the biosynthesis of tRNA t6A in Escherichia coli
    • Zhang,W., Collinet,B., Perrochia,L., Durand,D. and van Tilbeurgh,H. (2015) The ATP-mediated formation of the YgjD-YeaZ-YjeE complex is required for the biosynthesis of tRNA t6A in Escherichia coli. Nucleic Acids Res., 43, 1804-1817.
    • (2015) Nucleic Acids Res. , vol.43 , pp. 1804-1817
    • Zhang, W.1    Collinet, B.2    Perrochia, L.3    Durand, D.4    Van Tilbeurgh, H.5
  • 12
    • 35548949828 scopus 로고    scopus 로고
    • An archaeal orthologue of the universal protein Kae1 is an iron metalloprotein which exhibits atypical DNA-binding properties and apurinic-endonuclease activity in vitro
    • Hecker,A., Leulliot,N., Gadelle,D., Graille,M., Justome,A., Dorlet,P., Brochier,C., Quevillon-Cheruel,S., Le Cam,E., van Tilbeurgh,H. et al. (2007) An archaeal orthologue of the universal protein Kae1 is an iron metalloprotein which exhibits atypical DNA-binding properties and apurinic-endonuclease activity in vitro. Nucleic Acids Res., 35, 6042-6051.
    • (2007) Nucleic Acids Res. , vol.35 , pp. 6042-6051
    • Hecker, A.1    Leulliot, N.2    Gadelle, D.3    Graille, M.4    Justome, A.5    Dorlet, P.6    Brochier, C.7    Quevillon-Cheruel, S.8    Le Cam, E.9    Van Tilbeurgh, H.10
  • 13
    • 84878279469 scopus 로고    scopus 로고
    • Crystal structure of the dimer of two essential Salmonella typhimurium proteins, YgjD & YeaZ and calorimetric evidence for the formation of a ternary YgjD-YeaZ-YjeE complex
    • Nichols,C.E., Lamb,H.K., Thompson,P., Omari,K.E., Lockyer,M., Charles,I., Hawkins,A.R. and Stammers,D.K. (2013) Crystal structure of the dimer of two essential Salmonella typhimurium proteins, YgjD & YeaZ and calorimetric evidence for the formation of a ternary YgjD-YeaZ-YjeE complex. Protein Sci., 22, 628-640.
    • (2013) Protein Sci. , vol.22 , pp. 628-640
    • Nichols, C.E.1    Lamb, H.K.2    Thompson, P.3    Omari, K.E.4    Lockyer, M.5    Charles, I.6    Hawkins, A.R.7    Stammers, D.K.8
  • 14
    • 0035158122 scopus 로고    scopus 로고
    • Urkinase: Structure of acetate kinase, a member of the ASKHA superfamily of phosphotransferases
    • Buss,K.A., Cooper,D.R., Ingram-Smith,C., Ferry,J.G., Sanders,D.A. and Hasson,M.S. (2001) Urkinase: structure of acetate kinase, a member of the ASKHA superfamily of phosphotransferases. J. Bacteriol., 183, 680-686.
    • (2001) J. Bacteriol. , vol.183 , pp. 680-686
    • Buss, K.A.1    Cooper, D.R.2    Ingram-Smith, C.3    Ferry, J.G.4    Sanders, D.A.5    Hasson, M.S.6
  • 15
    • 59749094748 scopus 로고    scopus 로고
    • Theuniversal Kae1 protein and the associated Bud32 kinase (PRPK), a mysteriousprotein couple probably essential for genome maintenance in Archaea andEukarya
    • Hecker,H., Graille,M., Madec,E, Gadelle,D., Lecam,E., van Tilbeurgh,H. and Forterre,P.2009)Theuniversal Kae1 protein and the associated Bud32 kinase (PRPK), a mysteriousprotein couple probably essential for genome maintenance in Archaea andEukarya. Biochem Soc Trans., 37, 29-35.
    • (2009) Biochem Soc Trans. , vol.37 , pp. 29-35
    • Hecker, H.1    Graille, M.2    Madec, E.3    Gadelle, D.4    Lecam, E.5    Van Tilbeurgh, H.6    Forterre, P.7
  • 16
    • 51049107924 scopus 로고    scopus 로고
    • Structure of the archaeal Kae1/Bud32 fusion protein MJ1130: A model for the eukaryotic EKC/KEOPS subcomplex
    • Hecker,A., Lopreiato,R., Graille,M., Collinet,B., Forterre,P., Libri,D. and van Tilbeurgh,H. (2008) Structure of the archaeal Kae1/Bud32 fusion protein MJ1130: a model for the eukaryotic EKC/KEOPS subcomplex. EMBO J., 27, 2340-2351.
    • (2008) EMBO J. , vol.27 , pp. 2340-2351
    • Hecker, A.1    Lopreiato, R.2    Graille, M.3    Collinet, B.4    Forterre, P.5    Libri, D.6    Van Tilbeurgh, H.7
  • 18
    • 27844479168 scopus 로고    scopus 로고
    • A family portrait of the RIO kinases
    • LaRonde-LeBlanc,N. and Wlodawer,A. (2005) A family portrait of the RIO kinases. J. Biol. Chem., 280, 37297-37300.
    • (2005) J. Biol. Chem. , vol.280 , pp. 37297-37300
    • LaRonde-LeBlanc, N.1    Wlodawer, A.2
  • 20
    • 0034007384 scopus 로고    scopus 로고
    • Highly hydrophilic proteins in prokaryotes and eukaryotes are common during conditions of water deficit
    • Garay-Arroyo,A., Colmenero-Flores,J.M., Garciarrubio,A. and Covarrubias,A.A. (2000) Highly hydrophilic proteins in prokaryotes and eukaryotes are common during conditions of water deficit. J. Biol. Chem., 275, 5668-5674.
    • (2000) J. Biol. Chem. , vol.275 , pp. 5668-5674
    • Garay-Arroyo, A.1    Colmenero-Flores, J.M.2    Garciarrubio, A.3    Covarrubias, A.A.4
  • 21
    • 23944515281 scopus 로고    scopus 로고
    • A genome-wide screen for Saccharomyces cerevisiae nonessential genes involved in mannosyl phosphate transfer to mannoprotein-linked oligosaccharides
    • Corbacho,I., Olivero,I. and Hernandez,L.M. (2005) A genome-wide screen for Saccharomyces cerevisiae nonessential genes involved in mannosyl phosphate transfer to mannoprotein-linked oligosaccharides. Fungal Genet. Biol., 42, 773-790.
    • (2005) Fungal Genet. Biol. , vol.42 , pp. 773-790
    • Corbacho, I.1    Olivero, I.2    Hernandez, L.M.3
  • 22
    • 0035830494 scopus 로고    scopus 로고
    • Cdc13 delivers separate complexes to the telomere for end protection and replication
    • Pennock,E., Buckley,K. and Lundblad,V. (2001) Cdc13 delivers separate complexes to the telomere for end protection and replication. Cell, 104, 387-396.
    • (2001) Cell , vol.104 , pp. 387-396
    • Pennock, E.1    Buckley, K.2    Lundblad, V.3
  • 25
    • 33846811598 scopus 로고    scopus 로고
    • High-density yeast-tiling array reveals previously undiscovered introns and extensive regulation of meiotic splicing
    • Juneau,K., Palm,C., Miranda,M. and Davis,R.W. (2007) High-density yeast-tiling array reveals previously undiscovered introns and extensive regulation of meiotic splicing. Proc. Natl. Acad. Sci. U.S.A., 104, 1522-1527.
    • (2007) Proc. Natl. Acad. Sci. U.S.A. , vol.104 , pp. 1522-1527
    • Juneau, K.1    Palm, C.2    Miranda, M.3    Davis, R.W.4
  • 27
    • 0027879008 scopus 로고
    • Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants
    • Kabsch,W. (1993) Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants. J. Appl. Crystallogr., 26, 795-800.
    • (1993) J. Appl. Crystallogr. , vol.26 , pp. 795-800
    • Kabsch, W.1
  • 29
    • 0242460576 scopus 로고    scopus 로고
    • Generation, representation and flow of phase information in structure determination: Recent developments in and around SHARP 2.0
    • Bricogne,G., Vonrhein,C., Flensburg,C., Schiltz,M. and Paciorek,W. (2003) Generation, representation and flow of phase information in structure determination: recent developments in and around SHARP 2.0. Acta Crystallogr. D Biol. Crystallogr., 59, 2023-2030.
    • (2003) Acta Crystallogr. D Biol. Crystallogr. , vol.59 , pp. 2023-2030
    • Bricogne, G.1    Vonrhein, C.2    Flensburg, C.3    Schiltz, M.4    Paciorek, W.5
  • 31
    • 0032964481 scopus 로고    scopus 로고
    • Automated protein model building combined with iterative structure refinement
    • Perrakis,A., Morris,R. and Lamzin,V.S. (1999) Automated protein model building combined with iterative structure refinement. Nat. Struct. Biol., 6, 458-463.
    • (1999) Nat. Struct. Biol. , vol.6 , pp. 458-463
    • Perrakis, A.1    Morris, R.2    Lamzin, V.S.3
  • 33
    • 0034517589 scopus 로고    scopus 로고
    • An approach to multi-copy search in molecular replacement
    • Vagin,A. and Teplyakov,A. (2000) An approach to multi-copy search in molecular replacement. Acta Crystallogr. D Biol. Crystallogr., 56, 1622-1624.
    • (2000) Acta Crystallogr. D Biol. Crystallogr. , vol.56 , pp. 1622-1624
    • Vagin, A.1    Teplyakov, A.2
  • 38
    • 77950793231 scopus 로고    scopus 로고
    • Experimental phasing with SHELXC/D/E: Combining chain tracing with density modification
    • Sheldrick,G.M. (2010) Experimental phasing with SHELXC/D/E: combining chain tracing with density modification. Acta Crystallogr. D Biol. Crystallogr., 66, 479-485.
    • (2010) Acta Crystallogr. D Biol. Crystallogr. , vol.66 , pp. 479-485
    • Sheldrick, G.M.1
  • 40
    • 77950798648 scopus 로고    scopus 로고
    • Recent developments in classical density modification
    • Cowtan,K. (2010) Recent developments in classical density modification. Acta Crystallogr. D Biol. Crystallogr., 66, 470-478.
    • (2010) Acta Crystallogr. D Biol. Crystallogr. , vol.66 , pp. 470-478
    • Cowtan, K.1
  • 45
    • 63849246525 scopus 로고    scopus 로고
    • Protein structure prediction on the Web: A case study using the Phyre server
    • Kelley,L.A. and Sternberg,M.J. (2009) Protein structure prediction on the Web: a case study using the Phyre server. Nat. Protoc., 4, 363-371.
    • (2009) Nat. Protoc. , vol.4 , pp. 363-371
    • Kelley, L.A.1    Sternberg, M.J.2
  • 46
    • 70349316826 scopus 로고    scopus 로고
    • Combined sampler robot and high-performance liquid chromatography: A fully automated system for biological small-angle X-ray scattering experiments at the Synchrotron SOLEIL SWING beamline
    • David,G. and Perez,J. (2009) Combined sampler robot and high-performance liquid chromatography: a fully automated system for biological small-angle X-ray scattering experiments at the Synchrotron SOLEIL SWING beamline. J. Appl. Crystallogr., 42, 892-900.
    • (2009) J. Appl. Crystallogr. , vol.42 , pp. 892-900
    • David, G.1    Perez, J.2
  • 47
    • 0035010533 scopus 로고    scopus 로고
    • Determination of domain structure of proteins from X-ray solution scattering
    • Svergun,D.I., Petoukhov,M.V. and Koch,M.H. (2001) Determination of domain structure of proteins from X-ray solution scattering. Biophys. J., 80, 2946-2953.
    • (2001) Biophys. J. , vol.80 , pp. 2946-2953
    • Svergun, D.I.1    Petoukhov, M.V.2    Koch, M.H.3
  • 49
    • 23244455562 scopus 로고    scopus 로고
    • Global rigid body modeling of macromolecular complexes against small-angle scattering data
    • Petoukhov,M.V. and Svergun,D.I. (2005) Global rigid body modeling of macromolecular complexes against small-angle scattering data. Biophys. J., 89, 1237-1250.
    • (2005) Biophys. J. , vol.89 , pp. 1237-1250
    • Petoukhov, M.V.1    Svergun, D.I.2
  • 50
    • 84880134130 scopus 로고    scopus 로고
    • High-quality protein backbone reconstruction from alpha carbons using Gaussian mixture models
    • Moore,B.L., Kelley,L.A., Barber,J., Murray,J.W. and MacDonald,J.T. (2013) High-quality protein backbone reconstruction from alpha carbons using Gaussian mixture models. J. Comput. Chem., 34, 1881-1889.
    • (2013) J. Comput. Chem. , vol.34 , pp. 1881-1889
    • Moore, B.L.1    Kelley, L.A.2    Barber, J.3    Murray, J.W.4    MacDonald, J.T.5
  • 51
    • 0029185933 scopus 로고
    • CRYSOL - A program to evaluate X-ray solution scattering of biological macromolecules from atomic coordinates
    • Svergun,D., Barberato,C. and Koch,M.H.J. (1995) CRYSOL - a program to evaluate X-ray solution scattering of biological macromolecules from atomic coordinates. J. Appl. Crystallogr., 28, 768-773.
    • (1995) J. Appl. Crystallogr. , vol.28 , pp. 768-773
    • Svergun, D.1    Barberato, C.2    Koch, M.H.J.3
  • 52
    • 35548949828 scopus 로고    scopus 로고
    • An archaeal orthologue of the universal protein Kae1 is an iron metalloprotein which exhibits atypical DNA-binding properties and apurinic-endonuclease activity in vitro
    • Hecker,A., Leulliot,N., Gadelle,D., Graille,M., Justome,A., Dorlet,P., Brochier,C., Quevillon-Cheruel,S., Le Cam,E., van Tilbeurgh,H. et al. (2007) An archaeal orthologue of the universal protein Kae1 is an iron metalloprotein which exhibits atypical DNA-binding properties and apurinic-endonuclease activity in vitro. Nucleic Acids Res., 35, 6042-6051.
    • (2007) Nucleic Acids Res. , vol.35 , pp. 6042-6051
    • Hecker, A.1    Leulliot, N.2    Gadelle, D.3    Graille, M.4    Justome, A.5    Dorlet, P.6    Brochier, C.7    Quevillon-Cheruel, S.8    Le Cam, E.9    Van Tilbeurgh, H.10
  • 55
    • 29144535787 scopus 로고    scopus 로고
    • The RIO kinases: An atypical protein kinase family required for ribosome biogenesis and cell cycle progression
    • LaRonde-LeBlanc,N. and Wlodawer,A. (2005) The RIO kinases: an atypical protein kinase family required for ribosome biogenesis and cell cycle progression. Biochim. Biophys. Acta, 1754, 14-24.
    • (2005) Biochim. Biophys. Acta , vol.1754 , pp. 14-24
    • LaRonde-LeBlanc, N.1    Wlodawer, A.2
  • 57


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.