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Volumn 75, Issue 1, 2011, Pages 89-94

Expression, purification and crystallization of adenosine 1408 aminoglycoside-resistance rRNA methyltransferases for structural studies

Author keywords

16S RNA; Antibiotic resistance; Bacteria; Methyltransferase; Ribosome

Indexed keywords

BACTERIAL PROTEIN; ESCHERICHIA COLI PROTEIN; KAMB PROTEIN, STREPTOMYCES TENEBRARIUS; METHYLTRANSFERASE; NPMA PROTEIN, E COLI; RECOMBINANT PROTEIN; RNA 16S;

EID: 78049307438     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.pep.2010.07.005     Document Type: Article
Times cited : (13)

References (19)
  • 1
    • 33644547013 scopus 로고    scopus 로고
    • Molecular understanding of aminoglycoside action and resistance
    • S. Jana, and J.K. Deb Molecular understanding of aminoglycoside action and resistance Appl. Microbiol. Biotechnol. 70 2006 140 150
    • (2006) Appl. Microbiol. Biotechnol. , vol.70 , pp. 140-150
    • Jana, S.1    Deb, J.K.2
  • 2
    • 70449717476 scopus 로고    scopus 로고
    • Determination of the target nucleosides for members of two families of 16S rRNA methyltransferases that confer resistance to partially overlapping groups of aminoglycoside antibiotics
    • M. Savic, J. Lovric, T.I. Tomic, B. Vasiljevic, and G.L. Conn Determination of the target nucleosides for members of two families of 16S rRNA methyltransferases that confer resistance to partially overlapping groups of aminoglycoside antibiotics Nucleic Acids Res. 37 2009 5420 5431
    • (2009) Nucleic Acids Res. , vol.37 , pp. 5420-5431
    • Savic, M.1    Lovric, J.2    Tomic, T.I.3    Vasiljevic, B.4    Conn, G.L.5
  • 3
    • 0024459873 scopus 로고
    • How antibiotic-producing organisms avoid suicide
    • E. Cundliffe How antibiotic-producing organisms avoid suicide Annu. Rev. Microbiol. 43 1989 207 233
    • (1989) Annu. Rev. Microbiol. , vol.43 , pp. 207-233
    • Cundliffe, E.1
  • 6
    • 77955084302 scopus 로고    scopus 로고
    • Structural basis for the methylation of G1405 in 16S rRNA by aminoglycoside resistance methyltransferase Sgm from an antibiotic producer: A diversity of active sites in m7G methyltransferases
    • doi:10.1093/nar/gkq1122
    • N. Husain, K.L. Tkaczuk, S.R. Tulsidas, K.H. Kaminska, S. Cubrilo, G. Maravic-Vlahovicek, J.M. Bujnicki, J. Sivaraman, Structural basis for the methylation of G1405 in 16S rRNA by aminoglycoside resistance methyltransferase Sgm from an antibiotic producer: a diversity of active sites in m7G methyltransferases. Nucleic Acids Res. (2010). doi:10.1093/nar/gkq1122.
    • (2010) Nucleic Acids Res.
    • Husain, N.1    Tkaczuk, K.L.2    Tulsidas, S.R.3    Kaminska, K.H.4    Cubrilo, S.5    Maravic-Vlahovicek, G.6    Bujnicki, J.M.7    Sivaraman, J.8
  • 7
    • 64649099870 scopus 로고    scopus 로고
    • Structural bases for 16 S rRNA methylation catalyzed by ArmA and RmtB methyltransferases
    • E. Schmitt, M. Galimand, M. Panvert, P. Courvalin, and Y. Mechulam Structural bases for 16 S rRNA methylation catalyzed by ArmA and RmtB methyltransferases J. Mol. Biol. 388 2009 570 582
    • (2009) J. Mol. Biol. , vol.388 , pp. 570-582
    • Schmitt, E.1    Galimand, M.2    Panvert, M.3    Courvalin, P.4    Mechulam, Y.5
  • 8
    • 0025813219 scopus 로고
    • Cloning of an aminoglycoside-resistance-encoding gene, KamC, from Saccharopolyspora hirsuta: Comparison with kamB from Streptomyces tenebrarius
    • D.J. Holmes, D. Drocourt, G. Tiraby, and E. Cundliffe Cloning of an aminoglycoside-resistance-encoding gene, KamC, from Saccharopolyspora hirsuta: comparison with kamB from Streptomyces tenebrarius Gene 102 1991 19 26
    • (1991) Gene , vol.102 , pp. 19-26
    • Holmes, D.J.1    Drocourt, D.2    Tiraby, G.3    Cundliffe, E.4
  • 9
    • 44449135212 scopus 로고    scopus 로고
    • Classification of 'Streptomyces tenebrarius' Higgins and Kastner as Streptoalloteichus tenebrarius nom. rev., comb. nov., and emended description of the genus Streptoalloteichus
    • T. Tamura, Y. Ishida, M. Otoguro, K. Hatano, and K. Suzuki Classification of 'Streptomyces tenebrarius' Higgins and Kastner as Streptoalloteichus tenebrarius nom. rev., comb. nov., and emended description of the genus Streptoalloteichus Int. J. Syst. Evol. Microbiol. 58 2008 688 691
    • (2008) Int. J. Syst. Evol. Microbiol. , vol.58 , pp. 688-691
    • Tamura, T.1    Ishida, Y.2    Otoguro, M.3    Hatano, K.4    Suzuki, K.5
  • 10
    • 36749013556 scopus 로고    scopus 로고
    • Novel plasmid-mediated 16S rRNA m1A1408 methyltransferase, NpmA, found in a clinically isolated Escherichia coli strain resistant to structurally diverse aminoglycosides
    • J. Wachino, K. Shibayama, H. Kurokawa, K. Kimura, K. Yamane, S. Suzuki, N. Shibata, Y. Ike, and Y. Arakawa Novel plasmid-mediated 16S rRNA m1A1408 methyltransferase, NpmA, found in a clinically isolated Escherichia coli strain resistant to structurally diverse aminoglycosides Antimicrob. Agents Chemother. 51 2007 4401 4409
    • (2007) Antimicrob. Agents Chemother. , vol.51 , pp. 4401-4409
    • Wachino, J.1    Shibayama, K.2    Kurokawa, H.3    Kimura, K.4    Yamane, K.5    Suzuki, S.6    Shibata, N.7    Ike, Y.8    Arakawa, Y.9
  • 11
    • 34548267221 scopus 로고    scopus 로고
    • Identification of a missing sequence and functionally important residues of 16S rRNA: M(1)A1408 methyltransferase KamB that causes bacterial resistance to aminoglycoside antibiotics
    • L. Koscinski, M. Feder, and J.M. Bujnicki Identification of a missing sequence and functionally important residues of 16S rRNA: m(1)A1408 methyltransferase KamB that causes bacterial resistance to aminoglycoside antibiotics Cell Cycle 6 2007 1268 1271
    • (2007) Cell Cycle , vol.6 , pp. 1268-1271
    • Koscinski, L.1    Feder, M.2    Bujnicki, J.M.3
  • 13
    • 14844294424 scopus 로고    scopus 로고
    • Protein production by auto-induction in high-density shaking cultures
    • F.W. Studier Protein production by auto-induction in high-density shaking cultures Protein Expr. Purif. 41 2005 207 234
    • (2005) Protein Expr. Purif. , vol.41 , pp. 207-234
    • Studier, F.W.1
  • 14
    • 0022470564 scopus 로고
    • Rapid chemical probing of conformation in 16 S ribosomal RNA and 30 S ribosomal subunits using primer extension
    • D. Moazed, S. Stern, and H.F. Noller Rapid chemical probing of conformation in 16 S ribosomal RNA and 30 S ribosomal subunits using primer extension J. Mol. Biol. 187 1986 399 416
    • (1986) J. Mol. Biol. , vol.187 , pp. 399-416
    • Moazed, D.1    Stern, S.2    Noller, H.F.3
  • 15
    • 45849096536 scopus 로고    scopus 로고
    • Protein secondary structure analyses from circular dichroism spectroscopy: Methods and reference databases
    • L. Whitmore, and B.A. Wallace Protein secondary structure analyses from circular dichroism spectroscopy: methods and reference databases Biopolymers 89 2008 392 400
    • (2008) Biopolymers , vol.89 , pp. 392-400
    • Whitmore, L.1    Wallace, B.A.2
  • 16
    • 0034672325 scopus 로고    scopus 로고
    • Estimation of protein secondary structure from CD spectra: Comparison of CONTIN, SELCON and CDSSTR methods with an expanded reference set
    • N. Sreerama, and R.W. Woody Estimation of protein secondary structure from CD spectra: comparison of CONTIN, SELCON and CDSSTR methods with an expanded reference set Anal. Biochem. 287 2000 252 260
    • (2000) Anal. Biochem. , vol.287 , pp. 252-260
    • Sreerama, N.1    Woody, R.W.2
  • 17
    • 50249152954 scopus 로고    scopus 로고
    • Critical residues for cofactor binding and catalytic activity in the aminoglycoside resistance methyltransferase Sgm
    • M. Savic, T. Ilic-Tomic, R. Macmaster, B. Vasiljevic, and G.L. Conn Critical residues for cofactor binding and catalytic activity in the aminoglycoside resistance methyltransferase Sgm J. Bacteriol. 190 2008 5855 5861
    • (2008) J. Bacteriol. , vol.190 , pp. 5855-5861
    • Savic, M.1    Ilic-Tomic, T.2    MacMaster, R.3    Vasiljevic, B.4    Conn, G.L.5
  • 19
    • 67650544978 scopus 로고    scopus 로고
    • Structure of the thiostrepton resistance methyltransferase-S-adenosyl-l- methionine complex and its interaction with ribosomal RNA
    • M.S. Dunstan, P.C. Hang, N.V. Zelinskaya, J.F. Honek, and G.L. Conn Structure of the thiostrepton resistance methyltransferase-S-adenosyl-l- methionine complex and its interaction with ribosomal RNA J. Biol. Chem. 284 2009 17013 17020
    • (2009) J. Biol. Chem. , vol.284 , pp. 17013-17020
    • Dunstan, M.S.1    Hang, P.C.2    Zelinskaya, N.V.3    Honek, J.F.4    Conn, G.L.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.