메뉴 건너뛰기




Volumn 17, Issue 3, 2009, Pages 374-385

Structural Basis for Binding of RNA and Cofactor by a KsgA Methyltransferase

Author keywords

PROTEINS; RNA

Indexed keywords

METHYLTRANSFERASE; PROTEIN KSGA; RNA; S ADENOSYLHOMOCYSTEINE; S ADENOSYLMETHIONINE; UNCLASSIFIED DRUG;

EID: 61449176110     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.str.2009.01.010     Document Type: Article
Times cited : (26)

References (57)
  • 4
    • 0031547961 scopus 로고    scopus 로고
    • Solution structure of the conserved 16 S-like ribosomal RNA UGAA tetraloop
    • Butcher S.E., Dieckmann T., and Feigon J. Solution structure of the conserved 16 S-like ribosomal RNA UGAA tetraloop. J. Mol. Biol. 268 (1997) 348-358
    • (1997) J. Mol. Biol. , vol.268 , pp. 348-358
    • Butcher, S.E.1    Dieckmann, T.2    Feigon, J.3
  • 5
    • 33751521683 scopus 로고    scopus 로고
    • Evidence for an early gene duplication event in the evolution of the mitochondrial transcription factor B family and maintenance of rRNA methyltransferase activity in human mtTFB1 and mtTFB2
    • Cotney J., and Shadel G.S. Evidence for an early gene duplication event in the evolution of the mitochondrial transcription factor B family and maintenance of rRNA methyltransferase activity in human mtTFB1 and mtTFB2. J. Mol. Evol. 63 (2006) 707-717
    • (2006) J. Mol. Evol. , vol.63 , pp. 707-717
    • Cotney, J.1    Shadel, G.S.2
  • 6
    • 33646128243 scopus 로고    scopus 로고
    • The adenosine dimethyltransferase KsgA recognizes a specific conformational state of the 30S ribosomal subunit
    • Desai P.M., and Rife J.P. The adenosine dimethyltransferase KsgA recognizes a specific conformational state of the 30S ribosomal subunit. Arch. Biochem. Biophys. 449 (2006) 57-63
    • (2006) Arch. Biochem. Biophys. , vol.449 , pp. 57-63
    • Desai, P.M.1    Rife, J.P.2
  • 8
    • 0034746572 scopus 로고    scopus 로고
    • Structure of the N6-adenine DNA methyltransferase M.TaqI in complex with DNA and a cofactor analog
    • Goedecke K., Pignot M., Goody R.S., Scheidig A.J., and Weinhold E. Structure of the N6-adenine DNA methyltransferase M.TaqI in complex with DNA and a cofactor analog. Nat. Struct. Biol. 8 (2001) 121-125
    • (2001) Nat. Struct. Biol. , vol.8 , pp. 121-125
    • Goedecke, K.1    Pignot, M.2    Goody, R.S.3    Scheidig, A.J.4    Weinhold, E.5
  • 10
    • 0015121549 scopus 로고
    • Change in methylation of 16S ribosomal RNA associated with mutation to kasugamycin resistance in Escherichia coli
    • Helser T.L., Davies J.E., and Dahlberg J.E. Change in methylation of 16S ribosomal RNA associated with mutation to kasugamycin resistance in Escherichia coli. Nat. New Biol. 233 (1971) 12-14
    • (1971) Nat. New Biol. , vol.233 , pp. 12-14
    • Helser, T.L.1    Davies, J.E.2    Dahlberg, J.E.3
  • 11
    • 0015494418 scopus 로고
    • Mechanism of kasugamycin resistance in Escherichia coli
    • Helser T.L., Davies J.E., and Dahlberg J.E. Mechanism of kasugamycin resistance in Escherichia coli. Nat. New Biol. 235 (1972) 6-9
    • (1972) Nat. New Biol. , vol.235 , pp. 6-9
    • Helser, T.L.1    Davies, J.E.2    Dahlberg, J.E.3
  • 12
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron-density maps and the location of errors in these models
    • Jones T.A., Zou J.Y., Cowan S.W., and Kjeldgaard M. Improved methods for building protein models in electron-density maps and the location of errors in these models. Acta Crystallogr. A 47 (1991) 110-119
    • (1991) Acta Crystallogr. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 13
    • 0028010888 scopus 로고
    • HhaI methyltransferase flips its target base out of the DNA helix
    • Klimasauskas S., Kumar S., Roberts R.J., and Cheng X. HhaI methyltransferase flips its target base out of the DNA helix. Cell 76 (1994) 357-369
    • (1994) Cell , vol.76 , pp. 357-369
    • Klimasauskas, S.1    Kumar, S.2    Roberts, R.J.3    Cheng, X.4
  • 14
    • 0016764579 scopus 로고
    • Minimal post-transcriptional modification of yeast mitochondrial ribosomal RNA
    • Klootwijk J., Klein I., and Grivell L.A. Minimal post-transcriptional modification of yeast mitochondrial ribosomal RNA. J. Mol. Biol. 97 (1975) 337-350
    • (1975) J. Mol. Biol. , vol.97 , pp. 337-350
    • Klootwijk, J.1    Klein, I.2    Grivell, L.A.3
  • 15
    • 0030766064 scopus 로고    scopus 로고
    • Substrate DNA and cofactor regulate the activities of a multi-functional restriction-modification enzyme, BcgI
    • Kong H., and Smith C.L. Substrate DNA and cofactor regulate the activities of a multi-functional restriction-modification enzyme, BcgI. Nucleic Acids Res. 25 (1997) 3687-3692
    • (1997) Nucleic Acids Res. , vol.25 , pp. 3687-3692
    • Kong, H.1    Smith, C.L.2
  • 16
    • 0027946731 scopus 로고
    • Three-dimensional structure of the adenine-specific DNA methyltransferase M.Taq I in complex with the cofactor S-adenosylmethionine
    • Labahn J., Granzin J., Schluckebier G., Robinson D.P., Jack W.E., Schildkraut I., and Saenger W. Three-dimensional structure of the adenine-specific DNA methyltransferase M.Taq I in complex with the cofactor S-adenosylmethionine. Proc. Natl. Acad. Sci. USA 91 (1994) 10957-10961
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 10957-10961
    • Labahn, J.1    Granzin, J.2    Schluckebier, G.3    Robinson, D.P.4    Jack, W.E.5    Schildkraut, I.6    Saenger, W.7
  • 17
    • 0028086499 scopus 로고
    • The Dim1 gene responsible for the conserved M(2)(6)Am(2)(6)a dimethylation in the 3′-terminal loop of 18-S ribosomal-RNA is essential in yeast
    • Lafontaine D., Delcour J., Glasser A.L., Desgres J., and Vandenhaute J. The Dim1 gene responsible for the conserved M(2)(6)Am(2)(6)a dimethylation in the 3′-terminal loop of 18-S ribosomal-RNA is essential in yeast. J. Mol. Biol. 241 (1994) 492-497
    • (1994) J. Mol. Biol. , vol.241 , pp. 492-497
    • Lafontaine, D.1    Delcour, J.2    Glasser, A.L.3    Desgres, J.4    Vandenhaute, J.5
  • 18
    • 0028866774 scopus 로고
    • The 18S ribosomal-RNA dimethylase Dim1p is required for pre-ribosomal-RNA processing in yeast
    • Lafontaine D., Vandenhaute J., and Tollervey D. The 18S ribosomal-RNA dimethylase Dim1p is required for pre-ribosomal-RNA processing in yeast. Genes Dev. 9 (1995) 2470-2481
    • (1995) Genes Dev. , vol.9 , pp. 2470-2481
    • Lafontaine, D.1    Vandenhaute, J.2    Tollervey, D.3
  • 19
    • 0031944479 scopus 로고    scopus 로고
    • Yeast 18S rRNA dimethylase Dim1p: a quality control mechanism in ribosome synthesis?
    • Lafontaine D.L.J., Preiss T., and Tollervey D. Yeast 18S rRNA dimethylase Dim1p: a quality control mechanism in ribosome synthesis?. Mol. Cell. Biol. 18 (1998) 2360-2370
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 2360-2370
    • Lafontaine, D.L.J.1    Preiss, T.2    Tollervey, D.3
  • 20
  • 21
    • 0031813880 scopus 로고    scopus 로고
    • Cell cycle-regulated processing of HEF1 to multiple protein forms differentially targeted to multiple subcellular compartments
    • Law S.F., Zhang Y.Z., Klein-Szanto A.J., and Golemis E.A. Cell cycle-regulated processing of HEF1 to multiple protein forms differentially targeted to multiple subcellular compartments. Mol. Cell. Biol. 18 (1998) 3540-3551
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 3540-3551
    • Law, S.F.1    Zhang, Y.Z.2    Klein-Szanto, A.J.3    Golemis, E.A.4
  • 22
    • 0028841409 scopus 로고
    • Structure-guided analysis reveals nine sequence motifs conserved among DNA amino-methyltransferases, and suggests a catalytic mechanism for these enzymes
    • Malone T., Blumenthal R.M., and Cheng X. Structure-guided analysis reveals nine sequence motifs conserved among DNA amino-methyltransferases, and suggests a catalytic mechanism for these enzymes. J. Mol. Biol. 253 (1995) 618-632
    • (1995) J. Mol. Biol. , vol.253 , pp. 618-632
    • Malone, T.1    Blumenthal, R.M.2    Cheng, X.3
  • 23
    • 0142138438 scopus 로고    scopus 로고
    • Alanine-scanning mutagenesis of the predicted rRNA-binding domain of ErmC′ redefines the substrate-binding site and suggests a model for protein-RNA interactions
    • Maravic G., Bujnicki J.M., Feder M., Pongor S., and Flogel M. Alanine-scanning mutagenesis of the predicted rRNA-binding domain of ErmC′ redefines the substrate-binding site and suggests a model for protein-RNA interactions. Nucleic Acids Res. 31 (2003) 4941-4949
    • (2003) Nucleic Acids Res. , vol.31 , pp. 4941-4949
    • Maravic, G.1    Bujnicki, J.M.2    Feder, M.3    Pongor, S.4    Flogel, M.5
  • 24
    • 0042736455 scopus 로고    scopus 로고
    • Mutational analysis defines the roles of conserved amino acid residues in the predicted catalytic pocket of the rRNA:m6A methyltransferase ErmC′
    • Maravic G., Feder M., Pongor S., Flogel M., and Bujnicki J.M. Mutational analysis defines the roles of conserved amino acid residues in the predicted catalytic pocket of the rRNA:m6A methyltransferase ErmC′. J. Mol. Biol. 332 (2003) 99-109
    • (2003) J. Mol. Biol. , vol.332 , pp. 99-109
    • Maravic, G.1    Feder, M.2    Pongor, S.3    Flogel, M.4    Bujnicki, J.M.5
  • 26
    • 0036148610 scopus 로고    scopus 로고
    • A human mitochondrial transcription factor is related to RNA adenine methyltransferases and binds S-adenosylmethionine
    • McCulloch V., Seidel-Rogol B.L., and Shadel G.S. A human mitochondrial transcription factor is related to RNA adenine methyltransferases and binds S-adenosylmethionine. Mol. Cell. Biol. 22 (2002) 1116-1125
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 1116-1125
    • McCulloch, V.1    Seidel-Rogol, B.L.2    Shadel, G.S.3
  • 27
    • 0026529433 scopus 로고
    • Identification of intermolecular RNA cross-links at the subunit interface of the Escherichia coli ribosome
    • Mitchell P., Osswald M., and Brimacombe R. Identification of intermolecular RNA cross-links at the subunit interface of the Escherichia coli ribosome. Biochemistry 31 (1992) 3004-3011
    • (1992) Biochemistry , vol.31 , pp. 3004-3011
    • Mitchell, P.1    Osswald, M.2    Brimacombe, R.3
  • 29
    • 28844481147 scopus 로고    scopus 로고
    • Solubility-enhancing proteins MBP and NusA play a passive role in the folding of their fusion partners
    • Nallamsetty S., and Waugh D.S. Solubility-enhancing proteins MBP and NusA play a passive role in the folding of their fusion partners. Protein Expr. Purif. 45 (2006) 175-182
    • (2006) Protein Expr. Purif. , vol.45 , pp. 175-182
    • Nallamsetty, S.1    Waugh, D.S.2
  • 30
    • 2342650072 scopus 로고    scopus 로고
    • Crystal structure of KsgA, a universally conserved rRNA adenine dimethyltransferase in Escherichia coli
    • O'Farrell H.C., Scarsdale J.N., and Rife J.P. Crystal structure of KsgA, a universally conserved rRNA adenine dimethyltransferase in Escherichia coli. J. Mol. Biol. 339 (2004) 337-353
    • (2004) J. Mol. Biol. , vol.339 , pp. 337-353
    • O'Farrell, H.C.1    Scarsdale, J.N.2    Rife, J.P.3
  • 31
    • 33646179813 scopus 로고    scopus 로고
    • Recognition of a complex substrate by the KsgA/Dim1 family of enzymes has been conserved throughout evolution
    • O'Farrell H.C., Pulicherla N., Desai P.M., and Rife J.P. Recognition of a complex substrate by the KsgA/Dim1 family of enzymes has been conserved throughout evolution. RNA 12 (2006) 725-733
    • (2006) RNA , vol.12 , pp. 725-733
    • O'Farrell, H.C.1    Pulicherla, N.2    Desai, P.M.3    Rife, J.P.4
  • 33
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski Z., and Minor W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276 (1997) 307-326
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 34
    • 0018698756 scopus 로고
    • Studies on the function of two adjacent N6,N6-dimethyladenosines near the 3′ end of 16 S ribosomal RNA of Escherichia coli. III. Purification and properties of the methylating enzyme and methylase-30 S interactions
    • Poldermans B., Roza L., and Van Knippenberg P.H. Studies on the function of two adjacent N6,N6-dimethyladenosines near the 3′ end of 16 S ribosomal RNA of Escherichia coli. III. Purification and properties of the methylating enzyme and methylase-30 S interactions. J. Biol. Chem. 254 (1979) 9094-9100
    • (1979) J. Biol. Chem. , vol.254 , pp. 9094-9100
    • Poldermans, B.1    Roza, L.2    Van Knippenberg, P.H.3
  • 35
    • 0018686494 scopus 로고
    • Studies on the function of two adjacent N6,N6-dimethyladenosines near the 3′ end of 16 S ribosomal RNA of Escherichia coli. II. The effect of the absence of the methyl groups on initiation of protein biosynthesis
    • Poldermans B., Van Buul C.P., and Van Knippenberg P.H. Studies on the function of two adjacent N6,N6-dimethyladenosines near the 3′ end of 16 S ribosomal RNA of Escherichia coli. II. The effect of the absence of the methyl groups on initiation of protein biosynthesis. J. Biol. Chem. 254 (1979) 9090-9093
    • (1979) J. Biol. Chem. , vol.254 , pp. 9090-9093
    • Poldermans, B.1    Van Buul, C.P.2    Van Knippenberg, P.H.3
  • 36
    • 0018868238 scopus 로고
    • Studies on the function of two adjacent N6,N6-dimethyladenosines near the 3′ end of 16S ribosomal RNA of Escherichia coli. IV. The effect of the methylgroups on ribosomal subunit interaction
    • Poldermans B., Bakker H., and Van Knippenberg P.H. Studies on the function of two adjacent N6,N6-dimethyladenosines near the 3′ end of 16S ribosomal RNA of Escherichia coli. IV. The effect of the methylgroups on ribosomal subunit interaction. Nucleic Acids Res. 8 (1980) 143-151
    • (1980) Nucleic Acids Res. , vol.8 , pp. 143-151
    • Poldermans, B.1    Bakker, H.2    Van Knippenberg, P.H.3
  • 37
    • 0033514427 scopus 로고    scopus 로고
    • Functional roles of the conserved aromatic amino acid residues at position 108 (motif IV) and position 196 (motif VIII) in base flipping and catalysis by the N6-adenine DNA methyltransferase from Thermus aquaticus
    • Pues H., Bleimling N., Holz B., Wolcke J., and Weinhold E. Functional roles of the conserved aromatic amino acid residues at position 108 (motif IV) and position 196 (motif VIII) in base flipping and catalysis by the N6-adenine DNA methyltransferase from Thermus aquaticus. Biochemistry 38 (1999) 1426-1434
    • (1999) Biochemistry , vol.38 , pp. 1426-1434
    • Pues, H.1    Bleimling, N.2    Holz, B.3    Wolcke, J.4    Weinhold, E.5
  • 38
    • 0032526960 scopus 로고    scopus 로고
    • The structure of a methylated tetraloop in 16S ribosomal RNA
    • Rife J.P., and Moore P.B. The structure of a methylated tetraloop in 16S ribosomal RNA. Structure 6 (1998) 747-756
    • (1998) Structure , vol.6 , pp. 747-756
    • Rife, J.P.1    Moore, P.B.2
  • 39
    • 0032504248 scopus 로고    scopus 로고
    • Functional roles of conserved amino acid residues in DNA methyltransferases investigated by site-directed mutagenesis of the EcoRV adenine-N6-methyltransferase
    • Roth M., Helm-Kruse S., Friedrich T., and Jeltsch A. Functional roles of conserved amino acid residues in DNA methyltransferases investigated by site-directed mutagenesis of the EcoRV adenine-N6-methyltransferase. J. Biol. Chem. 273 (1998) 17333-17342
    • (1998) J. Biol. Chem. , vol.273 , pp. 17333-17342
    • Roth, M.1    Helm-Kruse, S.2    Friedrich, T.3    Jeltsch, A.4
  • 40
    • 0031561804 scopus 로고    scopus 로고
    • Differential binding of S-adenosylmethionine S-adenosylhomocysteine and Sinefungin to the adenine-specific DNA methyltransferase M.TaqI
    • Schluckebier G., Kozak M., Bleimling N., Weinhold E., and Saenger W. Differential binding of S-adenosylmethionine S-adenosylhomocysteine and Sinefungin to the adenine-specific DNA methyltransferase M.TaqI. J. Mol. Biol. 265 (1997) 56-67
    • (1997) J. Mol. Biol. , vol.265 , pp. 56-67
    • Schluckebier, G.1    Kozak, M.2    Bleimling, N.3    Weinhold, E.4    Saenger, W.5
  • 41
    • 0033522646 scopus 로고    scopus 로고
    • The 2.2 Å structure of the rRNA methyltransferase ErmC′ and its complexes with cofactor and cofactor analogs: implications for the reaction mechanism
    • Schluckebier G., Zhong P., Stewart K.D., Kavanaugh T.J., and Abad-Zapatero C. The 2.2 Å structure of the rRNA methyltransferase ErmC′ and its complexes with cofactor and cofactor analogs: implications for the reaction mechanism. J. Mol. Biol. 289 (1999) 277-291
    • (1999) J. Mol. Biol. , vol.289 , pp. 277-291
    • Schluckebier, G.1    Zhong, P.2    Stewart, K.D.3    Kavanaugh, T.J.4    Abad-Zapatero, C.5
  • 42
    • 0034808120 scopus 로고    scopus 로고
    • Crystal structure of the transcription factor sc-mtTFB offers insights into mitochondrial transcription
    • Schubot F.D., Chen C.J., Rose J.P., Dailey T.A., Dailey H.A., and Wang B.C. Crystal structure of the transcription factor sc-mtTFB offers insights into mitochondrial transcription. Protein Sci. 10 (2001) 1980-1988
    • (2001) Protein Sci. , vol.10 , pp. 1980-1988
    • Schubot, F.D.1    Chen, C.J.2    Rose, J.P.3    Dailey, T.A.4    Dailey, H.A.5    Wang, B.C.6
  • 44
    • 0037228525 scopus 로고    scopus 로고
    • Human mitochondrial transcription factor B1 methylates ribosomal RNA at a conserved stem-loop
    • Seidel-Rogol B.L., McCulloch V., and Shadel G.S. Human mitochondrial transcription factor B1 methylates ribosomal RNA at a conserved stem-loop. Nat. Genet. 33 (2003) 23-24
    • (2003) Nat. Genet. , vol.33 , pp. 23-24
    • Seidel-Rogol, B.L.1    McCulloch, V.2    Shadel, G.S.3
  • 45
    • 0021064473 scopus 로고
    • Site of action of a ribosomal RNA methylase responsible for resistance to erythromycin and other antibiotics
    • Skinner R., Cundliffe E., and Schmidt F.J. Site of action of a ribosomal RNA methylase responsible for resistance to erythromycin and other antibiotics. J. Biol. Chem. 258 (1983) 12702-12706
    • (1983) J. Biol. Chem. , vol.258 , pp. 12702-12706
    • Skinner, R.1    Cundliffe, E.2    Schmidt, F.J.3
  • 46
    • 0016321036 scopus 로고
    • Methylation of 16S RNA during ribosome assembly in vitro
    • Thammana P., and Held W.A. Methylation of 16S RNA during ribosome assembly in vitro. Nature 251 (1974) 682-686
    • (1974) Nature , vol.251 , pp. 682-686
    • Thammana, P.1    Held, W.A.2
  • 47
    • 0032076832 scopus 로고    scopus 로고
    • Chloroplast development at low temperatures requires a homolog of DIM1, a yeast gene encoding the 18S rRNA dimethylase
    • Tokuhisa J.G., Vijayan P., Feldmann K.A., and Browse J.A. Chloroplast development at low temperatures requires a homolog of DIM1, a yeast gene encoding the 18S rRNA dimethylase. Plant Cell 10 (1998) 699-711
    • (1998) Plant Cell , vol.10 , pp. 699-711
    • Tokuhisa, J.G.1    Vijayan, P.2    Feldmann, K.A.3    Browse, J.A.4
  • 49
    • 0022347064 scopus 로고
    • Nucleotide sequence of the ksgA gene of Escherichia coli: comparison of methyltransferases effecting dimethylation of adenosine in ribosomal RNA
    • van Buul C.P., and van Knippenberg P.H. Nucleotide sequence of the ksgA gene of Escherichia coli: comparison of methyltransferases effecting dimethylation of adenosine in ribosomal RNA. Gene 38 (1985) 65-72
    • (1985) Gene , vol.38 , pp. 65-72
    • van Buul, C.P.1    van Knippenberg, P.H.2
  • 50
    • 0020606884 scopus 로고
    • Kasugamycin resistant mutants of Bacillus stearothermophilus lacking the enzyme for the methylation of two adjacent adenosines in 16S ribosomal RNA
    • Van Buul C.P., Damm J.B., and Van Knippenberg P.H. Kasugamycin resistant mutants of Bacillus stearothermophilus lacking the enzyme for the methylation of two adjacent adenosines in 16S ribosomal RNA. Mol. Gen. Genet. 189 (1983) 475-478
    • (1983) Mol. Gen. Genet. , vol.189 , pp. 475-478
    • Van Buul, C.P.1    Damm, J.B.2    Van Knippenberg, P.H.3
  • 51
    • 0024397726 scopus 로고
    • Autogenous regulation of the Escherichia coli ksgA gene at the level of translation
    • van Gemen B., Twisk J., and van Knippenberg P.H. Autogenous regulation of the Escherichia coli ksgA gene at the level of translation. J. Bacteriol. 171 (1989) 4002-4008
    • (1989) J. Bacteriol. , vol.171 , pp. 4002-4008
    • van Gemen, B.1    Twisk, J.2    van Knippenberg, P.H.3
  • 52
    • 0021771170 scopus 로고
    • Phylogeny of the conserved 3′ terminal structure of the RNA of small ribosomal subunits
    • Van Knippenberg P.H., Van Kimmenade J.M., and Heus H.A. Phylogeny of the conserved 3′ terminal structure of the RNA of small ribosomal subunits. Nucleic Acids Res. 12 (1984) 2595-2604
    • (1984) Nucleic Acids Res. , vol.12 , pp. 2595-2604
    • Van Knippenberg, P.H.1    Van Kimmenade, J.M.2    Heus, H.A.3
  • 53
    • 0028963496 scopus 로고
    • Erythromycin resistance by ribosome modification
    • Weisblum B. Erythromycin resistance by ribosome modification. Antimicrob. Agents Chemother. 39 (1995) 577-585
    • (1995) Antimicrob. Agents Chemother. , vol.39 , pp. 577-585
    • Weisblum, B.1
  • 54
    • 0028074254 scopus 로고
    • A mutational analysis of the two motifs common to adenine methyltransferases
    • Willcock D.F., Dryden D.T., and Murray N.E. A mutational analysis of the two motifs common to adenine methyltransferases. EMBO J. 13 (1994) 3902-3908
    • (1994) EMBO J. , vol.13 , pp. 3902-3908
    • Willcock, D.F.1    Dryden, D.T.2    Murray, N.E.3
  • 56
    • 43249093216 scopus 로고    scopus 로고
    • A conserved rRNA methyltransferase regulates ribosome biogenesis
    • Xu Z., O'Farrell H.C., Rife J.P., and Culver G.M. A conserved rRNA methyltransferase regulates ribosome biogenesis. Nat. Struct. Mol. Biol. 15 (2008) 534-536
    • (2008) Nat. Struct. Mol. Biol. , vol.15 , pp. 534-536
    • Xu, Z.1    O'Farrell, H.C.2    Rife, J.P.3    Culver, G.M.4
  • 57
    • 0030902818 scopus 로고    scopus 로고
    • Solution structure of an rRNA methyltransferase (ErmAM) that confers macrolide-lincosamide-streptogramin antibiotic resistance
    • Yu L., Petros A.M., Schnuchel A., Zhong P., Severin J.M., Walter K., Holzman T.F., and Fesik S.W. Solution structure of an rRNA methyltransferase (ErmAM) that confers macrolide-lincosamide-streptogramin antibiotic resistance. Nat. Struct. Biol. 4 (1997) 483-489
    • (1997) Nat. Struct. Biol. , vol.4 , pp. 483-489
    • Yu, L.1    Petros, A.M.2    Schnuchel, A.3    Zhong, P.4    Severin, J.M.5    Walter, K.6    Holzman, T.F.7    Fesik, S.W.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.