메뉴 건너뛰기




Volumn 16, Issue 6, 2011, Pages 5168-5181

Identification of N6,N6-dimethyladenosine in transfer RNA from Mycobacterium bovis bacille calmette-guérin

Author keywords

BCG; Mycobacteriaum bovis; Ribonucleoside modification; TRNA

Indexed keywords

ADENOSINE; DRUG DERIVATIVE; TRANSFER RNA;

EID: 79959627017     PISSN: None     EISSN: 14203049     Source Type: Journal    
DOI: 10.3390/molecules16065168     Document Type: Article
Times cited : (25)

References (33)
  • 2
    • 13444266430 scopus 로고    scopus 로고
    • The Small Subunit rRNA Modification Database
    • DOI 10.1093/nar/gki015
    • McCloskey, J.A.; Rozenski, J. The small subunit rRNA modification database. Nucl. Acid. Res. 2005, 33, D135-D138. (Pubitemid 40207846)
    • (2005) Nucleic Acids Research , vol.33 , Issue.DATABASE ISS.
    • McCloskey, J.A.1    Rozenski, J.2
  • 4
    • 0345060040 scopus 로고    scopus 로고
    • Novel Methyltransferase for Modified Uridine Residues at the Wobble Position of tRNA
    • DOI 10.1128/MCB.23.24.9283-9292.2003
    • Kalhor, H.R.; Clarke, S. Novel methyltransferase for modified uridine residues at the wobble position of tRNA. Mol. Cell. Biol. 2003, 23, 9283-9292. (Pubitemid 37499815)
    • (2003) Molecular and Cellular Biology , vol.23 , Issue.24 , pp. 9283-9292
    • Kalhor, H.R.1    Clarke, S.2
  • 5
    • 17844373810 scopus 로고    scopus 로고
    • 7G methyltransferase Trm8p/Trm82p: Evidence linking activity to a growth phenotype and implicating Trm82p in maintaining levels of active Trm8p
    • DOI 10.1261/rna.2030705
    • Alexandrov, A.; Grayhack, E.J.; Phizicky, E.M. tRNA m7G methyltransferase Trm8p/Trm82p: Evidence linking activity to a growth phenotype and implicating Trm82p in maintaining levels of active Trm8p. RNA 2005, 11, 821-830. (Pubitemid 40594346)
    • (2005) RNA , vol.11 , Issue.5 , pp. 821-830
    • Alexandrov, A.1    Grayhack, E.J.2    Phizicky, E.M.3
  • 7
    • 78650683942 scopus 로고    scopus 로고
    • A quantitative systems approach reveals dynamic control of tRNA modifications during cellular stress
    • Chan, C.T.; Dyavaiah, M.; DeMott, M.S.; Taghizadeh, K.; Dedon, P.C.; Begley, T.J. A quantitative systems approach reveals dynamic control of tRNA modifications during cellular stress. PLoS Genet. 2010, 6, e1001247.
    • (2010) PLoS Genet. , vol.6
    • Chan, C.T.1    Dyavaiah, M.2    DeMott, M.S.3    Taghizadeh, K.4    Dedon, P.C.5    Begley, T.J.6
  • 9
    • 0004104929 scopus 로고    scopus 로고
    • World Health Organization, G.T.P., Number WHO/HTM/TB/2009.411; Global Tuberculosis Programme, Geneva, Switzerland
    • World Health Organization, G.T.P. Global tuberculosis control: WHO report; Number WHO/HTM/TB/2009.411; Global Tuberculosis Programme, Geneva, Switzerland, 2009.
    • Global Tuberculosis Control: WHO Report , pp. 2009
  • 10
    • 0025715617 scopus 로고
    • Modern vaccines. Mycobacterial diseases
    • Fine, P.E.; Rodrigues, L.C. Modern vaccines. Mycobacterial diseases. Lancet 1990, 335, 1016-1020.
    • (1990) Lancet , vol.335 , pp. 1016-1020
    • Fine, P.E.1    Rodrigues, L.C.2
  • 11
    • 58149189877 scopus 로고    scopus 로고
    • GtRNAdb: A database of transfer RNA genes detected in genomic sequence
    • Chan, P.P.; Lowe, T.M. GtRNAdb: A database of transfer RNA genes detected in genomic sequence. Nucl. Acid. Res. 2009, 37, D93-D97.
    • (2009) Nucl. Acid. Res. , vol.37
    • Chan, P.P.1    Lowe, T.M.2
  • 13
    • 34548789633 scopus 로고    scopus 로고
    • Mass spectrometric identification and characterization of RNA-modifying enzymes
    • Suzuki, T.; Ikeuchi, Y.; Noma, A.; Sakaguchi, Y. Mass spectrometric identification and characterization of RNA-modifying enzymes. Methods Enzymol 2007, 425, 211-229.
    • (2007) Methods Enzymol , vol.425 , pp. 211-229
    • Suzuki, T.1    Ikeuchi, Y.2    Noma, A.3    Sakaguchi, Y.4
  • 14
    • 33745938634 scopus 로고    scopus 로고
    • Mass spectrometry of RNA: Linking the genome to the proteome
    • DOI 10.1093/bfgp/ell012, The Comparative and Functional Genomics (BITS) Workshop
    • Meng, Z.; Limbach, P.A. Mass spectrometry of RNA: Linking the genome to the proteome. Brief Funct Genomic Proteomic 2006, 5, 87-95. (Pubitemid 46403001)
    • (2006) Briefings in Functional Genomics and Proteomics , vol.5 , Issue.1 , pp. 87-95
    • Meng, Z.1    Limbach, P.A.2
  • 15
    • 27544446607 scopus 로고    scopus 로고
    • Study of the mass spectrometric fragmentation of pseudouridine: Comparison of fragmentation data obtained by matrix-assisted laser desorption/ionisation post-source decay, electrospray ion trap multistage mass spectrometry, and by a method utilising electrospray quadrupole time-of-flight tandem mass spectrometry and in-source fragmentation
    • DOI 10.1002/rcm.2151
    • Dudley, E.; Tuytten, R.; Bond, A.; Lemiere, F.; Brenton, A.G.; Esmans, E.L.; Newton, R.P. Study of the mass spectrometric fragmentation of pseudouridine: Comparison of fragmentation data obtained by matrix-assisted laser desorption/ionisation post-source decay, electrospray ion trap multistage mass spectrometry, and by a method utilising electrospray quadrupole time-of-flight tandem mass spectrometry and in-source fragmentation. Rapid Commun. Mass Spectrom 2005, 19, 3075-3085. (Pubitemid 41540735)
    • (2005) Rapid Communications in Mass Spectrometry , vol.19 , Issue.21 , pp. 3075-3085
    • Dudley, E.1    Tuytten, R.2    Bond, A.3    Lemiere, F.4    Brenton, A.G.5    Esmans, E.L.6    Newton, R.P.7
  • 16
    • 0026773531 scopus 로고
    • Collision-induced dissociation of adenine
    • to 3668
    • Nelson, C.C.M.; McCloskey, J.A. Collision-induced dissociation of adenine. J. Am. Chem. Soc. 1992, 114, 3661 to 3668.
    • (1992) J. Am. Chem. Soc. , vol.114 , pp. 3661
    • Nelson, C.C.M.1    McCloskey, J.A.2
  • 17
    • 0021752972 scopus 로고
    • Studies on 1-methyl adenine transfer RNA methyltransferase of Mycobacterium smegmatis
    • DOI 10.1007/BF00409778
    • Brahmachari, V.; Ramakrishnan, T. Studies on 1-methyl adenine transfer RNA methyltransferase of Mycobacterium smegmatis. Arch. Microbiol. 1984, 140, 91-95. (Pubitemid 15217066)
    • (1984) Archives of Microbiology , vol.140 , Issue.1 , pp. 91-95
    • Brahmachari, V.1    Ramakrishnan, T.2
  • 19
    • 0035955465 scopus 로고    scopus 로고
    • In silico analysis of the tRNA:m1A58 methyltransferase family: Homology-based fold prediction and identification of new members from Eubacteria and Archaea
    • DOI 10.1016/S0014-5793(01)02962-3, PII S0014579301029623
    • Bujnicki, J.M. In silico analysis of the tRNA:m1A58 methyltransferase family: Homology-based fold prediction and identification of new members from Eubacteria and Archaea. FEBS Lett. 2001, 507, 123-127. (Pubitemid 33001527)
    • (2001) FEBS Letters , vol.507 , Issue.2 , pp. 123-127
    • Bujnicki, J.M.1
  • 20
    • 0011572673 scopus 로고
    • The occurrence and distribution of thymine and three methylatedadenine bases in ribonucleic acids from several sources
    • Littlefield, J.W.; Dunn, D.B. The occurrence and distribution of thymine and three methylatedadenine bases in ribonucleic acids from several sources. Nature 1958, 181, 254-255.
    • (1958) Nature , vol.181 , pp. 254-255
    • Littlefield, J.W.1    Dunn, D.B.2
  • 22
    • 49949132862 scopus 로고
    • Minor nucleotide composition of ribosomal precursor, and ribosomal, ribonucleic acid in Escherichia coli
    • Dubin, D.T.; Günalp, A. Minor nucleotide composition of ribosomal precursor, and ribosomal, ribonucleic acid in Escherichia coli. Biochim. Biophys. Acta 1967, 134, 106-123.
    • (1967) Biochim. Biophys. Acta , vol.134 , pp. 106-123
    • Dubin, D.T.1    Günalp, A.2
  • 24
    • 0015939481 scopus 로고
    • Structure of an inducibly methylatable nucleotide sequence in 23S ribosomal ribonucleic acid from erythromycin-resistant Staphylococcus aureus
    • Lai, C.J.; Dahlberg, J.E.; Weisblum, B. Structure of an inducibly methylatable nucleotide sequence in 23S ribosomal ribonucleic acid from erythromycin-resistant Staphylococcus aureus. Biochemistry 1973, 12, 457-460.
    • (1973) Biochemistry , vol.12 , pp. 457-460
    • Lai, C.J.1    Dahlberg, J.E.2    Weisblum, B.3
  • 25
    • 9144227769 scopus 로고
    • The occurrence of methylated bases in ribosomal ribonucleic acid of Escherichia coli K12 W-6
    • Starr, J.L.; Fefferman, R. The occurrence of methylated bases in ribosomal ribonucleic acid of Escherichia coli K12 W-6. J. Biol. Chem. 1964, 239, 3457-3461.
    • (1964) J. Biol. Chem. , vol.239 , pp. 3457-3461
    • Starr, J.L.1    Fefferman, R.2
  • 26
    • 36749000444 scopus 로고    scopus 로고
    • Dissection of 16S rRNA methyltransferase (KsgA) function in Escherichia coli
    • DOI 10.1128/JB.01259-07
    • Inoue, K.; Basu, S.; Inouye, M. Dissection of 16S rRNA methyltransferase (KsgA) function in Escherichia coli. J. Bacteriol. 2007, 189, 8510-8518. (Pubitemid 350210020)
    • (2007) Journal of Bacteriology , vol.189 , Issue.23 , pp. 8510-8518
    • Inoue, K.1    Basu, S.2    Inouye, M.3
  • 27
    • 0015078149 scopus 로고
    • Erythromycin-inducible resistance in Staphylococcus aureus: Requirements for induction
    • Weisblum, B.; Siddhikol, C.; Lai, C.J.; Demohn, V. Erythromycin-inducible resistance in Staphylococcus aureus: Requirements for induction. J. Bacteriol. 1971, 106, 835-847.
    • (1971) J. Bacteriol. , vol.106 , pp. 835-847
    • Weisblum, B.1    Siddhikol, C.2    Lai, C.J.3    Demohn, V.4
  • 28
    • 0022180715 scopus 로고
    • Ribosomal RNA methylation in Staphylococcus aureus and Escherichia coli: Effect of the 'MLS' (erythromycin resistance) methylase
    • DOI 10.1016/0147-619X(85)90075-7
    • Thakker-Varia, S.; Ranzini, A.C.; Dubin, D.T. Ribosomal RNA methylation in Staphylococcus aureus and Escherichia coli: Effect of the "MLS" (erythromycin resistance) methylase. Plasmid 1985, 14, 152-161. (Pubitemid 16255073)
    • (1985) Plasmid , vol.14 , Issue.2 , pp. 152-161
    • Thakker-Varia, S.1    Ranzini, A.C.2    Dubin, D.T.3
  • 30
    • 33751157452 scopus 로고
    • 5U54)- methyltransferase
    • Gu, X.; Ofengand, J.; Santi, D.V. In vitro methylation of Escherichia coli 16S rRNA by tRNA (m5U54)-methyltransferase. Biochemistry 1994, 33, 2255-2261. (Pubitemid 24099625)
    • (1994) Biochemistry , vol.33 , Issue.8 , pp. 2255-2261
    • Gu, X.1    Ofengand, J.2    Santi, D.V.3
  • 32
    • 34548179680 scopus 로고    scopus 로고
    • Lipid peroxidation dominates the chemistry of DNA adduct formation in a mouse model of inflammation
    • DOI 10.1093/carcin/bgm037
    • Pang, B.; Zhou, X.; Yu, H.; Dong, M.; Taghizadeh, K.; Wishnok, J.S.; Tannenbaum, S.R.; Dedon, P.C. Lipid peroxidation dominates the chemistry of DNA adduct formation in a mouse model of inflammation. Carcinogenesis 2007, 28, 1807-1813. (Pubitemid 47303947)
    • (2007) Carcinogenesis , vol.28 , Issue.8 , pp. 1807-1813
    • Pang, B.1    Zhou, X.2    Yu, H.3    Dong, M.4    Taghizadeh, K.5    Wishnok, J.S.6    Tannenbaum, S.R.7    Dedon, P.C.8
  • 33
    • 50349091399 scopus 로고    scopus 로고
    • Quantification of DNA damage products resulting from deamination, oxidation and reaction with products of lipid peroxidation by liquid chromatography isotope dilution tandem mass spectrometry
    • Taghizadeh, K.; McFaline, J.L.; Pang, B.; Sullivan, M.; Dong, M.; Plummer, E.; Dedon, P.C. Quantification of DNA damage products resulting from deamination, oxidation and reaction with products of lipid peroxidation by liquid chromatography isotope dilution tandem mass spectrometry. Nat. Protoc. 2008, 3, 1287-1298.
    • (2008) Nat. Protoc. , vol.3 , pp. 1287-1298
    • Taghizadeh, K.1    McFaline, J.L.2    Pang, B.3    Sullivan, M.4    Dong, M.5    Plummer, E.6    Dedon, P.C.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.