메뉴 건너뛰기




Volumn 41, Issue 12, 2013, Pages 6332-6346

Reconstitution and characterization of eukaryotic N6-threonylcarbamoylation of tRNA using a minimal enzyme system

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; BUD32 PROTEIN; CELL PROTEIN; CGI121 PROTEIN; GON7 PROTEIN; HOMODIMER; KAE1 PROTEIN; PCC1 PROTEIN; QRI7 PROTEIN; SUA5 PROTEIN; TRANSFER RNA; UNCLASSIFIED DRUG; YEAZ PROTEIN; YGJD PROTEIN; YJEE PROTEIN;

EID: 84880242478     PISSN: 03051048     EISSN: 13624962     Source Type: Journal    
DOI: 10.1093/nar/gkt322     Document Type: Article
Times cited : (60)

References (48)
  • 3
    • 0019355045 scopus 로고
    • Effect of threonylcarbamoyl modification (t6A) in yeast tRNA Arg III on codon-anticodon and anticodon-anticodon interactions. A thermodynamic and kinetic evaluation
    • Weissenbach, J. and Grosjean, H. (1981) Effect of threonylcarbamoyl modification (t6A) in yeast tRNA Arg III on codon-anticodon and anticodon-anticodon interactions. A thermodynamic and kinetic evaluation. Eur. J. Biochem., 116, 207-213.
    • (1981) Eur. J. Biochem. , vol.116 , pp. 207-213
    • Weissenbach, J.1    Grosjean, H.2
  • 4
    • 33745126327 scopus 로고    scopus 로고
    • The naturally occurring N6-threonyl adenine in anticodon loop of Schizosaccharomyces pombe tRNAi causes formation of a unique U-turn motif
    • Lescrinier, E., Nauwelaerts, K., Zanier, K., Poesen, K., Sattler, M. and Herdewijn, P. (2006) The naturally occurring N6-threonyl adenine in anticodon loop of Schizosaccharomyces pombe tRNAi causes formation of a unique U-turn motif. Nucleic Acids Res., 34, 2878-2886.
    • (2006) Nucleic Acids Res. , vol.34 , pp. 2878-2886
    • Lescrinier, E.1    Nauwelaerts, K.2    Zanier, K.3    Poesen, K.4    Sattler, M.5    Herdewijn, P.6
  • 5
    • 84872686832 scopus 로고    scopus 로고
    • A cyclic form of N6-threonylcarbamoyladenosine as a widely distributed tRNA hypermodification
    • Miyauchi, K., Kimura, S. and Suzuki, T. (2013) A cyclic form of N6-threonylcarbamoyladenosine as a widely distributed tRNA hypermodification. Nat. Chem. Biol., 9, 105-111.
    • (2013) Nat. Chem. Biol. , vol.9 , pp. 105-111
    • Miyauchi, K.1    Kimura, S.2    Suzuki, T.3
  • 6
    • 73549090572 scopus 로고    scopus 로고
    • The Sua5 protein is essential for normal translational regulation in yeast
    • Lin, C.A., Ellis, S.R. and True, H.L. (2010) The Sua5 protein is essential for normal translational regulation in yeast. Mol. Cell. Biol., 30, 354-363.
    • (2010) Mol. Cell. Biol. , vol.30 , pp. 354-363
    • Lin, C.A.1    Ellis, S.R.2    True, H.L.3
  • 7
    • 0026322430 scopus 로고
    • Extragenic suppressors of a translation initiation defect in the cyc1 gene of Saccharomyces cerevisiae
    • Hampsey, M., Na, J.G., Pinto, I., Ware, D.E. and Berroteran, R.W. (1991) Extragenic suppressors of a translation initiation defect in the cyc1 gene of Saccharomyces cerevisiae. Biochimie, 73, 1445-1455.
    • (1991) Biochimie , vol.73 , pp. 1445-1455
    • Hampsey, M.1    Na, J.G.2    Pinto, I.3    Ware, D.E.4    Berroteran, R.W.5
  • 9
    • 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
  • 14
    • 77950543877 scopus 로고    scopus 로고
    • Sua5p is required for telomere recombination in Saccharomyces cerevisiae
    • Meng, F.L., Chen, X.F., Hu, Y., Tang, H.B., Dang, W. and Zhou, J.Q. (2010) Sua5p is required for telomere recombination in Saccharomyces cerevisiae. Cell Res., 20, 495-498.
    • (2010) Cell Res. , vol.20 , pp. 495-498
    • Meng, F.L.1    Chen, X.F.2    Hu, Y.3    Tang, H.B.4    Dang, W.5    Zhou, J.Q.6
  • 15
    • 67349168741 scopus 로고    scopus 로고
    • Sua5p a single-stranded telomeric DNA-binding protein facilitates telomere replication
    • Meng, F.L., Hu, Y., Shen, N., Tong, X.J., Wang, J., Ding, J. and Zhou, J.Q. (2009) Sua5p a single-stranded telomeric DNA-binding protein facilitates telomere replication. EMBO J., 28, 1466-1478.
    • (2009) EMBO J. , vol.28 , pp. 1466-1478
    • Meng, F.L.1    Hu, Y.2    Shen, N.3    Tong, X.J.4    Wang, J.5    Ding, J.6    Zhou, J.Q.7
  • 16
    • 36248953763 scopus 로고    scopus 로고
    • Impaired tRNA nuclear export links DNA damage and cell-cycle checkpoint
    • Ghavidel, A., Kislinger, T., Pogoutse, O., Sopko, R., Jurisica, I. and Emili, A. (2007) Impaired tRNA nuclear export links DNA damage and cell-cycle checkpoint. Cell, 131, 915-926.
    • (2007) Cell , vol.131 , pp. 915-926
    • Ghavidel, A.1    Kislinger, T.2    Pogoutse, O.3    Sopko, R.4    Jurisica, I.5    Emili, A.6
  • 19
    • 0024316220 scopus 로고
    • Prevention of translational frameshifting by the modified nucleoside 1-methylguanosine
    • Bjork, G.R., Wikstrom, P.M. and Bystrom, A.S. (1989) Prevention of translational frameshifting by the modified nucleoside 1-methylguanosine. Science, 244, 986-989.
    • (1989) Science , vol.244 , pp. 986-989
    • Bjork, G.R.1    Wikstrom, P.M.2    Bystrom, A.S.3
  • 20
  • 21
    • 0035801515 scopus 로고    scopus 로고
    • Improvement of reading frame maintenance is a common function for several tRNA modifications
    • Urbonavicius, J., Qian, Q., Durand, J.M., Hagervall, T.G. and Bjork, G.R. (2001) Improvement of reading frame maintenance is a common function for several tRNA modifications. EMBO J., 20, 4863-4873.
    • (2001) EMBO J. , vol.20 , pp. 4863-4873
    • Urbonavicius, J.1    Qian, Q.2    Durand, J.M.3    Hagervall, T.G.4    Bjork, G.R.5
  • 22
    • 84859994582 scopus 로고    scopus 로고
    • Biosynthesis of threonylcarbamoyl adenosine (t6A), a universal tRNA nucleoside
    • Deutsch, C., El Yacoubi, B., de Crecy-Lagard, V. and Iwata-Reuyl, D. (2012) 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
  • 24
    • 84868529691 scopus 로고    scopus 로고
    • Mechanism of N6-Threonylcarbamoyladenonsine (t(6)A) Biosynthesis: Isolation and Characterization of the Intermediate Threonylcarbamoyl-AMP
    • Lauhon, C.T. (2012) Mechanism of N6-Threonylcarbamoyladenonsine (t(6)A) Biosynthesis: Isolation and Characterization of the Intermediate Threonylcarbamoyl-AMP. Biochemistry, 51, 8950-8963.
    • (2012) Biochemistry , vol.51 , pp. 8950-8963
    • Lauhon, C.T.1
  • 25
    • 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
  • 28
    • 0024362769 scopus 로고
    • Ribonucleoside analysis by reversed-phase high-performance liquid chromatography
    • Gehrke, C.W. and Kuo, K.C. (1989) Ribonucleoside analysis by reversed-phase high-performance liquid chromatography. J. Chromatogr., 471, 3-36.
    • (1989) J. Chromatogr. , vol.471 , pp. 3-36
    • Gehrke, C.W.1    Kuo, K.C.2
  • 31
    • 0034009520 scopus 로고    scopus 로고
    • Size-distribution analysis of macromolecules by sedimentation velocity ultracentrifugation and lamm equation modeling
    • Schuck, P. (2000) Size-distribution analysis of macromolecules by sedimentation velocity ultracentrifugation and lamm equation modeling. Biophys. J., 78, 1606-1619.
    • (2000) Biophys. J. , vol.78 , pp. 1606-1619
    • Schuck, P.1
  • 34
    • 70350132871 scopus 로고    scopus 로고
    • Qri7/OSGEPL, the mitochondrial version of the universal Kae1/YgjD protein, is essential for mitochondrial genome maintenance
    • Oberto, J., Breuil, N., Hecker, A., Farina, F., Brochier-Armanet, C., Culetto, E. and Forterre, P. (2009) Qri7/OSGEPL, the mitochondrial version of the universal Kae1/YgjD protein, is essential for mitochondrial genome maintenance. Nucleic Acids Res., 37, 5343-5352.
    • (2009) Nucleic Acids Res. , vol.37 , pp. 5343-5352
    • Oberto, J.1    Breuil, N.2    Hecker, A.3    Farina, F.4    Brochier-Armanet, C.5    Culetto, E.6    Forterre, P.7
  • 35
    • 0015530484 scopus 로고
    • Biosynthesis and specific labeling of N-(purin-6-ylcarbamoyl)threonine of Escherichia coli transfer RNA
    • Powers, D.M. and Peterkofsky, A. (1972) Biosynthesis and specific labeling of N-(purin-6-ylcarbamoyl)threonine of Escherichia coli transfer RNA. Biochem. Biophys. Res. Commun., 46, 831-838.
    • (1972) Biochem. Biophys. Res. Commun. , vol.46 , pp. 831-838
    • Powers, D.M.1    Peterkofsky, A.2
  • 36
    • 0015329948 scopus 로고
    • Biosynthesis of N-(purin-6-ylcarbamoyl)-L-threonine riboside. Incorporation of L-threonine in vivo into modified nucleoside of transfer ribonucleic acid
    • Chheda, G.B., Hong, C.I., Piskorz, C.F. and Harmon, G.A. (1972) Biosynthesis of N-(purin-6-ylcarbamoyl)-L-threonine riboside. Incorporation of L-threonine in vivo into modified nucleoside of transfer ribonucleic acid. Biochem. J., 127, 515-519.
    • (1972) Biochem. J. , vol.127 , pp. 515-519
    • Chheda, G.B.1    Hong, C.I.2    Piskorz, C.F.3    Harmon, G.A.4
  • 38
    • 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
  • 39
    • 0014940137 scopus 로고
    • The isolation and characterization of N-[9-(beta-D-ribofuranosyl)-purin- 6-ylcarbamoyl]glycine from yeast transfer RNA
    • Schweizer, M.P., McGrath, K. and Baczynskyj, L. (1970) The isolation and characterization of N-[9-(beta-D-ribofuranosyl)-purin-6-ylcarbamoyl]glycine from yeast transfer RNA. Biochem. Biophys. Res. Commun., 40, 1046-1052.
    • (1970) Biochem. Biophys. Res. Commun. , vol.40 , pp. 1046-1052
    • Schweizer, M.P.1    McGrath, K.2    Baczynskyj, L.3
  • 40
    • 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
  • 43
    • 25144477805 scopus 로고    scopus 로고
    • Mechanistic link between PKR dimerization, autophosphorylation, and eIF2alpha substrate recognition
    • Dey, M., Cao, C., Dar, A.C., Tamura, T., Ozato, K., Sicheri, F. and Dever, T.E. (2005) Mechanistic link between PKR dimerization, autophosphorylation, and eIF2alpha substrate recognition. Cell, 122, 901-913.
    • (2005) Cell , vol.122 , pp. 901-913
    • Dey, M.1    Cao, C.2    Dar, A.C.3    Tamura, T.4    Ozato, K.5    Sicheri, F.6    Dever, T.E.7
  • 44
    • 25144502820 scopus 로고    scopus 로고
    • Higher-order substrate recognition of eIF2alpha by the RNA-dependent protein kinase PKR
    • Dar, A.C., Dever, T.E. and Sicheri, F. (2005) Higher-order substrate recognition of eIF2alpha by the RNA-dependent protein kinase PKR. Cell, 122, 887-900.
    • (2005) Cell , vol.122 , pp. 887-900
    • Dar, A.C.1    Dever, T.E.2    Sicheri, F.3
  • 45
    • 34250354002 scopus 로고    scopus 로고
    • Conserved intermolecular salt bridge required for activation of protein kinases PKR, GCN2, and PERK
    • Dey, M., Cao, C., Sicheri, F. and Dever, T.E. (2007) Conserved intermolecular salt bridge required for activation of protein kinases PKR, GCN2, and PERK. J. Biol. Chem., 282, 6653-6660.
    • (2007) J. Biol. Chem. , vol.282 , pp. 6653-6660
    • Dey, M.1    Cao, C.2    Sicheri, F.3    Dever, T.E.4
  • 46
    • 70349438995 scopus 로고    scopus 로고
    • A dimerization-dependent mechanism drives RAF catalytic activation
    • Rajakulendran, T., Sahmi, M., Lefrancois, M., Sicheri, F. and Therrien, M. (2009) A dimerization-dependent mechanism drives RAF catalytic activation. Nature, 461, 542-545.
    • (2009) Nature , vol.461 , pp. 542-545
    • Rajakulendran, T.1    Sahmi, M.2    Lefrancois, M.3    Sicheri, F.4    Therrien, M.5
  • 47
    • 33745002702 scopus 로고    scopus 로고
    • An allosteric mechanism for activation of the kinase domain of epidermal growth factor receptor
    • Zhang, X., Gureasko, J., Shen, K., Cole, P.A. and Kuriyan, J. (2006) An allosteric mechanism for activation of the kinase domain of epidermal growth factor receptor. Cell, 125, 1137-1149.
    • (2006) Cell , vol.125 , pp. 1137-1149
    • Zhang, X.1    Gureasko, J.2    Shen, K.3    Cole, P.A.4    Kuriyan, J.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.