메뉴 건너뛰기




Volumn 43, Issue 3, 2015, Pages 1804-1817

The ATP-mediated formation of the YgjD-YeaZ-YjeE complex is required for the biosynthesis of tRNA t6A in Escherichia coli

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE; ADENOSINE PHOSPHATE; ADENOSINE TRIPHOSPHATASE; ADENOSINE TRIPHOSPHATE; BICARBONATE; ESCHERICHIA COLI PROTEIN; HETERODIMER; N6 THREONYLCARBAMOYLADENOSINE; PROTEIN YEAZ; PROTEIN YGJD; PROTEIN YJEE; THREONINE; THREONYLCARBAMOYLADENYLATE; TRANSFER RNA; UNCLASSIFIED DRUG; ADENOSINE DIPHOSPHATE; BACTERIAL RNA; YEAZ PROTEIN, E COLI; YGJD PROTEIN, E COLI; YJEE PROTEIN, E COLI;

EID: 84936743574     PISSN: 03051048     EISSN: 13624962     Source Type: Journal    
DOI: 10.1093/nar/gku1397     Document Type: Article
Times cited : (38)

References (43)
  • 1
    • 71549130107 scopus 로고    scopus 로고
    • Do all modifications benefit all tRNAs?
    • Phizicky,E.M. and Alfonzo,J.D. (2010) Do all modifications benefit all tRNAs? FEBS Lett., 584, 265-271.
    • (2010) FEBS Lett. , vol.584 , pp. 265-271
    • Phizicky, E.M.1    Alfonzo, J.D.2
  • 3
    • 84870152928 scopus 로고    scopus 로고
    • Biosynthesis and function of posttranscriptional modifications of transfer RNAs
    • El Yacoubi,B., Bailly,M. and de Crecy-Lagard,V. (2012) Biosynthesis and function of posttranscriptional modifications of transfer RNAs. Annu. Rev. Genet., 46, 69-95.
    • (2012) Annu. Rev. Genet. , vol.46 , pp. 69-95
    • El Yacoubi, B.1    Bailly, M.2    De Crecy-Lagard, V.3
  • 4
    • 71849108697 scopus 로고    scopus 로고
    • Deciphering synonymous codons in the three domains of life: Co-evolution with specific tRNA modification enzymes
    • Grosjean,H., de Crecy-Lagard,V. and Marck,C. (2010) Deciphering synonymous codons in the three domains of life: co-evolution with specific tRNA modification enzymes. FEBS Lett., 584, 252-264.
    • (2010) FEBS Lett. , vol.584 , pp. 252-264
    • Grosjean, H.1    De Crecy-Lagard, V.2    Marck, C.3
  • 5
    • 0014679197 scopus 로고
    • Isolation and characterization of a novel nucleoside, N-[(9-beta-D-ribofuranosyl-9H-purin-6-yl)carbamoyl]threonine, from human urine
    • Chheda,G.B. (1969) Isolation and characterization of a novel nucleoside, N-[(9-beta-D-ribofuranosyl-9H-purin-6-yl)carbamoyl]threonine, from human urine. Life Sci., 8, 979-987.
    • (1969) Life Sci. , vol.8 , pp. 979-987
    • Chheda, G.B.1
  • 7
    • 20144367825 scopus 로고    scopus 로고
    • Structural effects of hypermodified nucleosides in the Escherichia coli and human tRNALys anticodon loop: The effect of nucleosides s2U, mcm5U, mcm5s2U, mnm5s2U, t6A, and ms2t6A
    • Durant,P.C., Bajji,A.C., Sundaram,M., Kumar,R.K. and Davis,D.R. (2005) Structural effects of hypermodified nucleosides in the Escherichia coli and human tRNALys anticodon loop: the effect of nucleosides s2U, mcm5U, mcm5s2U, mnm5s2U, t6A, and ms2t6A. Biochemistry, 44, 8078-8089.
    • (2005) Biochemistry , vol.44 , pp. 8078-8089
    • Durant, P.C.1    Bajji, A.C.2    Sundaram, M.3    Kumar, R.K.4    Davis, D.R.5
  • 8
    • 0031594815 scopus 로고    scopus 로고
    • The methyl group of the N6-methyl-N6-threonylcarbamoyladenosine in tRNA of Escherichia coli modestly improves the efficiency of the tRNA
    • Qian,Q., Curran,J.F. and Bjork,G.R. (1998) The methyl group of the N6-methyl-N6-threonylcarbamoyladenosine in tRNA of Escherichia coli modestly improves the efficiency of the tRNA. J. Bacteriol., 180, 1808-1813.
    • (1998) J. Bacteriol. , vol.180 , pp. 1808-1813
    • Qian, Q.1    Curran, J.F.2    Bjork, G.R.3
  • 9
    • 84872686832 scopus 로고    scopus 로고
    • A cyclic form of N(6)-threonylcarbamoyladenosine as a widely distributed tRNA hypermodification
    • Miyauchi,K., Kimura,S. and Suzuki,T. (2013) A cyclic form of N(6)-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
  • 11
    • 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
  • 13
    • 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
  • 14
    • 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
  • 18
    • 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
  • 19
    • 0942268722 scopus 로고    scopus 로고
    • Analysis of the interaction between piD261/Bud32, an evolutionarily conserved protein kinase of Saccharomyces cerevisiae, and the Grx4 glutaredoxin
    • Lopreiato,R., Facchin,S., Sartori,G., Arrigoni,G., Casonato,S., Ruzzene,M., Pinna,L.A. and Carignani,G. (2004) Analysis of the interaction between piD261/Bud32, an evolutionarily conserved protein kinase of Saccharomyces cerevisiae, and the Grx4 glutaredoxin. Biochem. J., 377, 395-405.
    • (2004) Biochem. J. , vol.377 , pp. 395-405
    • Lopreiato, R.1    Facchin, S.2    Sartori, G.3    Arrigoni, G.4    Casonato, S.5    Ruzzene, M.6    Pinna, L.A.7    Carignani, G.8
  • 22
    • 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
  • 24
    • 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
  • 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
  • 29
    • 83855165692 scopus 로고    scopus 로고
    • Extreme genome reduction in symbiotic bacteria
    • McCutcheon,J.P. and Moran,N.A. (2012) Extreme genome reduction in symbiotic bacteria. Nat. Rev. Microbiol., 10, 13-26.
    • (2012) Nat. Rev. Microbiol. , vol.10 , pp. 13-26
    • McCutcheon, J.P.1    Moran, N.A.2
  • 31
    • 33744832396 scopus 로고    scopus 로고
    • Structural characterization of Salmonella typhimurium YeaZ, an M22 O-sialoglycoprotein endopeptidase homolog
    • Nichols,C.E., Johnson,C., Lockyer,M., Charles,I.G., Lamb,H.K., Hawkins,A.R. and Stammers,D.K. (2006) Structural characterization of Salmonella typhimurium YeaZ, an M22 O-sialoglycoprotein endopeptidase homolog. Proteins, 64, 111-123.
    • (2006) Proteins , vol.64 , pp. 111-123
    • Nichols, C.E.1    Johnson, C.2    Lockyer, M.3    Charles, I.G.4    Lamb, H.K.5    Hawkins, A.R.6    Stammers, D.K.7
  • 32
    • 67849106093 scopus 로고    scopus 로고
    • Grasping at shadows: Revealing the elusive nature of essential genes
    • Msadek,T. (2009) Grasping at shadows: revealing the elusive nature of essential genes. J. Bacteriol., 191, 4701-4704.
    • (2009) J. Bacteriol. , vol.191 , pp. 4701-4704
    • Msadek, T.1
  • 34
    • 10944266372 scopus 로고    scopus 로고
    • Probing the active site of YjeE: A vital Escherichia coli protein of unknown function
    • Allali-Hassani,A., Campbell,T.L., Ho,A., Schertzer,J.W. and Brown,E.D. (2004) Probing the active site of YjeE: a vital Escherichia coli protein of unknown function. Biochem. J., 384, 577-584.
    • (2004) Biochem. J. , vol.384 , pp. 577-584
    • Allali-Hassani, A.1    Campbell, T.L.2    Ho, A.3    Schertzer, J.W.4    Brown, E.D.5
  • 35
    • 32044468906 scopus 로고    scopus 로고
    • Conserved P-loop GTPases of unknown function in bacteria: An emerging and vital ensemble in bacterial physiology
    • Brown,E.D. (2005) Conserved P-loop GTPases of unknown function in bacteria: an emerging and vital ensemble in bacterial physiology. Biochem. Cell Biol., 83, 738-746.
    • (2005) Biochem. Cell Biol. , vol.83 , pp. 738-746
    • Brown, E.D.1
  • 37
    • 67650865950 scopus 로고    scopus 로고
    • Simple and efficient site-directed mutagenesis using two single-primer reactions in parallel to generate mutants for protein structure-function studies
    • Edelheit,O., Hanukoglu,A. and Hanukoglu,I. (2009) Simple and efficient site-directed mutagenesis using two single-primer reactions in parallel to generate mutants for protein structure-function studies. BMC Biotechnol., 9, 61.
    • (2009) BMC Biotechnol. , vol.9 , pp. 61
    • Edelheit, O.1    Hanukoglu, A.2    Hanukoglu, I.3
  • 38
    • 0025690281 scopus 로고
    • Characterization of the ATP binding site on Escherichia coli DNA gyrase. Affinity labeling of Lys-103 and Lys-110 of the B subunit by pyridoxal 5′-diphospho-5′-adenosine
    • Tamura,J.K. and Gellert,M. (1990) Characterization of the ATP binding site on Escherichia coli DNA gyrase. Affinity labeling of Lys-103 and Lys-110 of the B subunit by pyridoxal 5′-diphospho-5′-adenosine. J. Biol. Chem., 265, 21342-21349.
    • (1990) J. Biol. Chem. , vol.265 , pp. 21342-21349
    • Tamura, J.K.1    Gellert, M.2
  • 39
    • 80051747844 scopus 로고    scopus 로고
    • Structural analysis of the essential resuscitation promoting factor YeaZ suggests a mechanism of nucleotide regulation through dimer reorganization
    • Aydin,I., Saijo-Hamano,Y., Namba,K., Thomas,C. and Roujeinikova,A. (2011) Structural analysis of the essential resuscitation promoting factor YeaZ suggests a mechanism of nucleotide regulation through dimer reorganization. PLoS One, 6, e23245.
    • (2011) PLoS One , vol.6
    • Aydin, I.1    Saijo-Hamano, Y.2    Namba, K.3    Thomas, C.4    Roujeinikova, A.5
  • 41
    • 84902492779 scopus 로고    scopus 로고
    • A complement to the modern crystallographer's toolbox: Caged gadolinium complexes with versatile binding modes
    • Stelter,M., Molina,R., Jeudy,S., Kahn,R., Abergel,C. and Hermoso,J.A. (2014) A complement to the modern crystallographer's toolbox: caged gadolinium complexes with versatile binding modes. Acta Crystallogr. D Biol. Crystallogr., 70, 1506-1516.
    • (2014) Acta Crystallogr. D Biol. Crystallogr. , vol.70 , pp. 1506-1516
    • Stelter, M.1    Molina, R.2    Jeudy, S.3    Kahn, R.4    Abergel, C.5    Hermoso, J.A.6
  • 42
    • 84874433733 scopus 로고    scopus 로고
    • Regulation of small GTPases by GEFs, GAPs, and GDIs
    • Cherfils,J. and Zeghouf,M. (2013) Regulation of small GTPases by GEFs, GAPs, and GDIs. Physiol. Rev., 93, 269-309.
    • (2013) Physiol. Rev. , vol.93 , pp. 269-309
    • Cherfils, J.1    Zeghouf, M.2
  • 43
    • 64049115730 scopus 로고    scopus 로고
    • The ATPase activity of an 'essential' Bacillus subtilis enzyme, YdiB, is required for its cellular function and is modulated by oligomerization
    • Karst,J.C., Foucher,A.E., Campbell,T.L., Di Guilmi,A.M., Stroebel,D., Mangat,C.S., Brown,E.D. and Jault,J.M. (2009) The ATPase activity of an 'essential' Bacillus subtilis enzyme, YdiB, is required for its cellular function and is modulated by oligomerization. Microbiology, 155, 944-956.
    • (2009) Microbiology , vol.155 , pp. 944-956
    • Karst, J.C.1    Foucher, A.E.2    Campbell, T.L.3    Di Guilmi, A.M.4    Stroebel, D.5    Mangat, C.S.6    Brown, E.D.7    Jault, J.M.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.