메뉴 건너뛰기




Volumn 73, Issue 1, 2010, Pages 83-89

Expression and purification of untagged and histidine-tagged folate-dependent tRNA:m5U54 methyltransferase from Bacillus subtilis

Author keywords

5 Methyluridine; Expression; Flavoenzyme; Histidine tag; Purification; Recombinant TrmFO protein; RNA methyltransferase

Indexed keywords

BACILLUS SUBTILIS; BACTERIA (MICROORGANISMS); ESCHERICHIA COLI;

EID: 77955415071     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.pep.2010.04.013     Document Type: Article
Times cited : (15)

References (24)
  • 1
    • 1242309517 scopus 로고    scopus 로고
    • Decoding the genome: A modified view
    • P.F. Agris, Decoding the genome: a modified view, Nucleic Acids Res. 32 (2004) 223-238.
    • (2004) Nucleic Acids Res. , vol.32 , pp. 223-238
    • Agris, P.F.1
  • 2
    • 0028650333 scopus 로고
    • Enzymatic mechanism of tRNA (m5U54)methyltransferase
    • J.T. Kealey, X. Gu, D.V. Santi, Enzymatic mechanism of tRNA (m5U54)methyltransferase, Biochimie 76 (1994) 1133-1142.
    • (1994) Biochimie , vol.76 , pp. 1133-1142
    • Kealey, J.T.1    Gu, X.2    Santi, D.V.3
  • 3
    • 44349185734 scopus 로고    scopus 로고
    • Structure of a TrmA- RNA complex: A consensus RNA fold contributes to substrate selectivity and catalysis in m5U methyltransferases
    • A. Alian, T.T. Lee, S.L. Griner, R.M. Stroud, J. Finer-Moore, Structure of a TrmA- RNA complex: a consensus RNA fold contributes to substrate selectivity and catalysis in m5U methyltransferases, Proc. Natl. Acad. Sci. USA 105 (2008) 6876-6881.
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 6876-6881
    • Alian, A.1    Lee, T.T.2    Griner, S.L.3    Stroud, R.M.4    Finer-Moore, J.5
  • 5
    • 50849135134 scopus 로고    scopus 로고
    • The crystal structure of Pyrococcus abyssi tRNA (uracil-54, C5)-methyltransferase provides insights into its tRNA specificity
    • H. Walbott, N. Leulliot, H. Grosjean, B. Golinelli-Pimpaneau, The crystal structure of Pyrococcus abyssi tRNA (uracil-54, C5)-methyltransferase provides insights into its tRNA specificity, Nucleic Acids Res. 36 (2008) 4929-4940.
    • (2008) Nucleic Acids Res. , vol.36 , pp. 4929-4940
    • Walbott, H.1    Leulliot, N.2    Grosjean, H.3    Golinelli-Pimpaneau, B.4
  • 6
    • 0016344184 scopus 로고
    • The occurrence of a transmethylation reaction not involving S-adenosylmethionine in the formation of ribothymidine in Bacillus subtilis transfer-RNA
    • J.M. Romeo, A.S. Delk, J.C. Rabinowitz, The occurrence of a transmethylation reaction not involving S-adenosylmethionine in the formation of ribothymidine in Bacillus subtilis transfer-RNA, Biochem. Biophys. Res. Commun. 61 (1974) 1256-1261.
    • (1974) Biochem. Biophys. Res. Commun. , vol.61 , pp. 1256-1261
    • Romeo, J.M.1    Delk, A.S.2    Rabinowitz, J.C.3
  • 7
    • 0016669480 scopus 로고
    • Biosynthesis of ribosylthymine in the transfer RNA of Streptococcus faecalis: A folate-dependent methylation not involving Sadenosylmethionine
    • A.S. Delk, J.C. Rabinowitz, Biosynthesis of ribosylthymine in the transfer RNA of Streptococcus faecalis: a folate-dependent methylation not involving Sadenosylmethionine, Proc. Natl. Acad. Sci. USA 72 (1975) 528-530.
    • (1975) Proc. Natl. Acad. Sci. USA , vol.72 , pp. 528-530
    • Delk, A.S.1    Rabinowitz, J.C.2
  • 8
    • 0017344847 scopus 로고
    • Tetrahydrofolate-dependent biosynthesis of ribothymidine in transfer ribonucleic acids of Gram-positive bacteria
    • W. Schmidt, H.H. Arnold, H. Kersten, Tetrahydrofolate-dependent biosynthesis of ribothymidine in transfer ribonucleic acids of Gram-positive bacteria, J. Bacteriol. 129 (1977) 15-21.
    • (1977) J. Bacteriol. , vol.129 , pp. 15-21
    • Schmidt, W.1    Arnold, H.H.2    Kersten, H.3
  • 9
    • 0018901584 scopus 로고
    • Methylenetetrahydrofolate-dependent biosynthesis of ribothymidine in transfer RNA of Streptococcus faecalis. Evidence for reduction of the 1-carbon unit by FADH2
    • A.S. Delk, D.P. Nagle Jr., J.C. Rabinowitz, Methylenetetrahydrofolate- dependent biosynthesis of ribothymidine in transfer RNA of Streptococcus faecalis. Evidence for reduction of the 1-carbon unit by FADH2, J. Biol. Chem. 255 (1980) 4387-4390.
    • (1980) J. Biol. Chem. , vol.255 , pp. 4387-4390
    • Delk, A.S.1    Nagle Jr., D.P.2    Rabinowitz, J.C.3
  • 10
    • 22844445708 scopus 로고    scopus 로고
    • Identification of a novel gene encoding a flavin-dependent tRNA:m5U methyltransferase in bacteria - evolutionary implications
    • J. Urbonavicius, S. Skouloubris, H. Myllykallio, H. Grosjean, Identification of a novel gene encoding a flavin-dependent tRNA:m5U methyltransferase in bacteria - evolutionary implications, Nucleic Acids Res. 33 (2005) 3955-3964.
    • (2005) Nucleic Acids Res. , vol.33 , pp. 3955-3964
    • Urbonavicius, J.1    Skouloubris, S.2    Myllykallio, H.3    Grosjean, H.4
  • 11
    • 40449104681 scopus 로고    scopus 로고
    • Crystallization and preliminary X-ray crystallographic characterization of TrmFO. A folate-dependent tRNA methyltransferase from Thermotoga maritima
    • N. Cicmil, Crystallization and preliminary X-ray crystallographic characterization of TrmFO. A folate-dependent tRNA methyltransferase from Thermotoga maritima, Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 64 (2008) 193-195.
    • (2008) Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. , vol.64 , pp. 193-195
    • Cicmil, N.1
  • 13
    • 44949138270 scopus 로고    scopus 로고
    • Crystal structures of the conserved tRNA-modifying enzyme GidA: Implications for its interaction with MnmE and substrate
    • S. Meyer, A. Scrima, W. Versees, A. Wittinghofer, Crystal structures of the conserved tRNA-modifying enzyme GidA: implications for its interaction with MnmE and substrate, J. Mol. Biol. 380 (2008) 532-547.
    • (2008) J. Mol. Biol. , vol.380 , pp. 532-547
    • Meyer, S.1    Scrima, A.2    Versees, W.3    Wittinghofer, A.4
  • 14
    • 73649122039 scopus 로고    scopus 로고
    • Evolutionarily conserved proteins MnmE and GidA catalyze the formation of two methyluridine derivatives at tRNA wobble positions
    • I. Moukadiri, S. Prado, J. Piera, A. Velazquez-Campoy, G.R. Bjérk, M.E. Armengod, Evolutionarily conserved proteins MnmE and GidA catalyze the formation of two methyluridine derivatives at tRNA wobble positions, Nucleic Acids Res. 37 (2009) 7177-7193.
    • (2009) Nucleic Acids Res. , vol.37 , pp. 7177-7193
    • Moukadiri, I.1    Prado, S.2    Piera, J.3    Velazquez-Campoy, A.4    Bjérk, G.R.5    Armengod, M.E.6
  • 15
    • 0033970608 scopus 로고    scopus 로고
    • New sequence motifs in flavoproteins: Evidence for common ancestry and tools to predict structure
    • O. Vallon, New sequence motifs in flavoproteins: evidence for common ancestry and tools to predict structure, Proteins 38 (2000) 95-114.
    • (2000) Proteins , vol.38 , pp. 95-114
    • Vallon, O.1
  • 16
    • 0034854206 scopus 로고    scopus 로고
    • Sequence-structure analysis of FAD-containing proteins
    • O. Dym, D. Eisenberg, Sequence-structure analysis of FAD-containing proteins, Protein Sci. 10 (2001) 1712-1728.
    • (2001) Protein Sci. , vol.10 , pp. 1712-1728
    • Dym, O.1    Eisenberg, D.2
  • 17
    • 40849085149 scopus 로고    scopus 로고
    • Effect of location of the His-tag on the production of soluble and functional Buthus martensii Karsch insect toxin
    • C.G. Xu, X.J. Fan, Y.J. Fu, A.H. Liang, Effect of location of the His-tag on the production of soluble and functional Buthus martensii Karsch insect toxin, Protein Expr. Purif. 59 (2008) 103-109.
    • (2008) Protein Expr. Purif. , vol.59 , pp. 103-109
    • Xu, C.G.1    Fan, X.J.2    Fu, Y.J.3    Liang, A.H.4
  • 18
    • 34548740836 scopus 로고    scopus 로고
    • In vitro detection of the enzymatic activity of folate-dependent tRNA (Uracil-54, C5)-methyltransferase: Evolutionary implications
    • J. Urbonavicius, C. Brochier-Armanet, S. Skouloubris, H. Myllykallio, H. Grosjean, In vitro detection of the enzymatic activity of folate-dependent tRNA (Uracil-54, C5)-methyltransferase: evolutionary implications, Methods Enzymol. 425 (2007) 103-119.
    • (2007) Methods Enzymol. , vol.425 , pp. 103-119
    • Urbonavicius, J.1    Brochier-Armanet, C.2    Skouloubris, S.3    Myllykallio, H.4    Grosjean, H.5
  • 19
    • 0026254055 scopus 로고
    • Parameters of helixcoil transition theory for alanine-based peptides of varying chain lengths in water
    • J.M. Scholtz, H. Qian, E.J. York, J.M. Stewart, R.L. Baldwin, Parameters of helixcoil transition theory for alanine-based peptides of varying chain lengths in water, Biopolymers 31 (1991) 1463-1470.
    • (1991) Biopolymers , vol.31 , pp. 1463-1470
    • Scholtz, J.M.1    Qian, H.2    York, E.J.3    Stewart, J.M.4    Baldwin, R.L.5
  • 20
    • 34548801413 scopus 로고    scopus 로고
    • Detection of enzymatic activity of transfer RNA modification enzymes using radiolabeled tRNA substrates
    • H. Grosjean, L. Droogmans, M. Roovers, G. Keith, Detection of enzymatic activity of transfer RNA modification enzymes using radiolabeled tRNA substrates, Methods Enzymol. 425 (2007) 55-101.
    • (2007) Methods Enzymol. , vol.425 , pp. 55-101
    • Grosjean, H.1    Droogmans, L.2    Roovers, M.3    Keith, G.4
  • 21
    • 0028053929 scopus 로고
    • Purification and properties of double-stranded RNAspecific adenosine deaminase from calf thymus
    • M.A. O'Connell, W. Keller, Purification and properties of double-stranded RNAspecific adenosine deaminase from calf thymus, Proc. Natl. Acad. Sci. USA 91 (1994) 10596-10600.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 10596-10600
    • O'Connell, M.A.1    Keller, W.2
  • 22
    • 0035718956 scopus 로고    scopus 로고
    • Expression of cloned cDNA for the human mitochondrial RNA polymerase in Escherichia coli and purification
    • S.C. Nam, C. Kang, Expression of cloned cDNA for the human mitochondrial RNA polymerase in Escherichia coli and purification, Protein Expr. Purif. 21 (2001) 485-491.
    • (2001) Protein Expr. Purif. , vol.21 , pp. 485-491
    • Nam, S.C.1    Kang, C.2
  • 23
    • 4644272663 scopus 로고    scopus 로고
    • Overexpression and affinity chromatography purification of the Type III restriction endonuclease EcoP15I for use in transcriptome analysis
    • E. Moncke-Buchner, P. Mackeldanz, D.H. Kruger, M. Reuter, Overexpression and affinity chromatography purification of the Type III restriction endonuclease EcoP15I for use in transcriptome analysis, J. Biotechnol. 114 (2004) 99-106.
    • (2004) J. Biotechnol. , vol.114 , pp. 99-106
    • Moncke-Buchner, E.1    Mackeldanz, P.2    Kruger, D.H.3    Reuter, M.4
  • 24
    • 0018158893 scopus 로고
    • Reversible resolution of flavoproteins into apoproteins and free flavins
    • M. Husain, V. Massey, Reversible resolution of flavoproteins into apoproteins and free flavins, Methods Enzymol. 53 (1978) 429-437.
    • (1978) Methods Enzymol. , vol.53 , pp. 429-437
    • Husain, M.1    Massey, V.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.