메뉴 건너뛰기




Volumn 13, Issue 11, 2007, Pages 1969-1976

Substrate specificity and properties of the Escherichia coli 16S rRNA methyltransferase, RsmE

Author keywords

E. coli; Methyltransferase; RNA modification; Small subunit

Indexed keywords

HISTIDINE; RIBOSOME RNA; RNA 16S; RNA METHYLTRANSFERASE; SPERMIDINE;

EID: 35549012369     PISSN: 13558382     EISSN: 14699001     Source Type: Journal    
DOI: 10.1261/rna.700507     Document Type: Article
Times cited : (22)

References (32)
  • 2
    • 33646806139 scopus 로고    scopus 로고
    • 5C methyltransferase specific for 16S rRNA nucleotide 1407
    • 5C methyltransferase specific for 16S rRNA nucleotide 1407. J. Mol. Biol. 3: 777-786.
    • (2006) J. Mol. Biol , vol.3 , pp. 777-786
    • Andersen, N.M.1    Douthwaite, S.2
  • 4
    • 33344476204 scopus 로고    scopus 로고
    • Identification and characterization of RsmE, the founding member of a new RNA base methyltransferase family
    • Basturea, G.N., Rudd, K.E., and Deutscher, M.P. 2006. Identification and characterization of RsmE, the founding member of a new RNA base methyltransferase family. RNA 12: 426-434.
    • (2006) RNA , vol.12 , pp. 426-434
    • Basturea, G.N.1    Rudd, K.E.2    Deutscher, M.P.3
  • 5
    • 33750488430 scopus 로고    scopus 로고
    • Structural basis for mRNA and tRNA positioning on the ribosome
    • Berk, V., Zang, W., Pai, R.D., and Cate, J.H. 2006. Structural basis for mRNA and tRNA positioning on the ribosome. Proc. Natl. Acad. Sci. 103: 15830-15834.
    • (2006) Proc. Natl. Acad. Sci , vol.103 , pp. 15830-15834
    • Berk, V.1    Zang, W.2    Pai, R.D.3    Cate, J.H.4
  • 6
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M.M. 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72: 248-254.
    • (1976) Anal. Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 7
    • 0036303417 scopus 로고    scopus 로고
    • Crystal structure of the 30S ribosomal subunit from Thermus thermophilus: Structure of the proteins and their interactions with 16S RNA
    • Brodersen, D.E., Clemons Jr., W.M., Carter, A.P., Wimberly, B.T., and Ramakrishnan, V. 2002. Crystal structure of the 30S ribosomal subunit from Thermus thermophilus: Structure of the proteins and their interactions with 16S RNA. J. Mol. Biol. 316: 725-768.
    • (2002) J. Mol. Biol , vol.316 , pp. 725-768
    • Brodersen, D.E.1    Clemons Jr., W.M.2    Carter, A.P.3    Wimberly, B.T.4    Ramakrishnan, V.5
  • 8
    • 0037319895 scopus 로고    scopus 로고
    • Assembly of the 30S ribosomal subunit
    • Culver, G.M. 2003. Assembly of the 30S ribosomal subunit. Biopolymers 68: 234-249.
    • (2003) Biopolymers , vol.68 , pp. 234-249
    • Culver, G.M.1
  • 9
    • 0025773644 scopus 로고
    • The absence of modified nucleotides affects both in vitro assembly and in vitro function of the 30S ribosomal subunit of Escherichia coli
    • Cunningham, P.R., Richard, R.B., Weitzmann, C.J., Nurse, K., and Ofengand, J. 1991. The absence of modified nucleotides affects both in vitro assembly and in vitro function of the 30S ribosomal subunit of Escherichia coli. Biochimie 73: 789-796.
    • (1991) Biochimie , vol.73 , pp. 789-796
    • Cunningham, P.R.1    Richard, R.B.2    Weitzmann, C.J.3    Nurse, K.4    Ofengand, J.5
  • 10
    • 0036629250 scopus 로고    scopus 로고
    • rRNA modifications and ribosome function
    • Decatur, W.A. and Fournier, M.J. 2002. rRNA modifications and ribosome function. Trends Biochem. Sci. 27: 344-351.
    • (2002) Trends Biochem. Sci , vol.27 , pp. 344-351
    • Decatur, W.A.1    Fournier, M.J.2
  • 11
    • 0024498489 scopus 로고
    • In vitro assembly of 30S and 70S bacterial ribosomes from 16S RNA containing single base substitutions, insertions, and deletions around the decoding site (C1400)
    • Denman, R., Weitzmann, C., Cunningham, P.R., Nergre, D., Nurse, K., Colgan, J., Pan, Y.C., Miedel, M., and Ofengand, J. 1989. In vitro assembly of 30S and 70S bacterial ribosomes from 16S RNA containing single base substitutions, insertions, and deletions around the decoding site (C1400). Biochemistry 28: 1002-1011.
    • (1989) Biochemistry , vol.28 , pp. 1002-1011
    • Denman, R.1    Weitzmann, C.2    Cunningham, P.R.3    Nergre, D.4    Nurse, K.5    Colgan, J.6    Pan, Y.C.7    Miedel, M.8    Ofengand, J.9
  • 12
    • 0141704142 scopus 로고    scopus 로고
    • Functional assignment based on structural analysis: Crystal structure of the yggJ protein (HI0303) of Haemophilus influenzae reveals an RNA methyltransferase with a deep trefoil knot
    • Forouhar, F., Shen, J., Xiao, R., Acton, T.B., Montelione, G.T., and Tong, L. 2003. Functional assignment based on structural analysis: Crystal structure of the yggJ protein (HI0303) of Haemophilus influenzae reveals an RNA methyltransferase with a deep trefoil knot. Proteins 53: 329-332.
    • (2003) Proteins , vol.53 , pp. 329-332
    • Forouhar, F.1    Shen, J.2    Xiao, R.3    Acton, T.B.4    Montelione, G.T.5    Tong, L.6
  • 13
    • 0024448151 scopus 로고
    • Calculation of protein extinction coefficients from amino acids sequence data
    • Gill, S.C. and von Hippel, P.H. 1989. Calculation of protein extinction coefficients from amino acids sequence data. Anal. Biochem. 182: 319-326.
    • (1989) Anal. Biochem , vol.182 , pp. 319-326
    • Gill, S.C.1    von Hippel, P.H.2
  • 14
    • 0036828880 scopus 로고    scopus 로고
    • Active site in RrmJ, a heat shock-induced methyltransferase
    • Hager, J., Staker, B.L., Bugl, H., and Jakob, U. 2002. Active site in RrmJ, a heat shock-induced methyltransferase. J. Biol. Chem. 277: 41978-41986.
    • (2002) J. Biol. Chem , vol.277 , pp. 41978-41986
    • Hager, J.1    Staker, B.L.2    Bugl, H.3    Jakob, U.4
  • 15
    • 4544273801 scopus 로고    scopus 로고
    • Substrate binding analysis of the 23S rRNA methyltransferase RrmJ
    • Hager, J., Staker, B.L., and Jakob, U. 2004. Substrate binding analysis of the 23S rRNA methyltransferase RrmJ. J. Bacteriol. 186: 6634-6642.
    • (2004) J. Bacteriol , vol.186 , pp. 6634-6642
    • Hager, J.1    Staker, B.L.2    Jakob, U.3
  • 17
    • 0014413537 scopus 로고
    • Release of ribosomal proteins from Escherichia coli ribosomes with high concentrations of lithium chloride
    • Itoh, T., Otaka, E., and Osawa, S. 1968. Release of ribosomal proteins from Escherichia coli ribosomes with high concentrations of lithium chloride. J. Mol. Biol. 33: 109-122.
    • (1968) J. Mol. Biol , vol.33 , pp. 109-122
    • Itoh, T.1    Otaka, E.2    Osawa, S.3
  • 18
    • 33748582906 scopus 로고    scopus 로고
    • Crystal structure of a 70S ribosome-tRNA complex reveals functional interactions and rearrangements
    • Korostelev, A., Trakhanov, S., Laurberg, M., and Noler, H.F. 2006. Crystal structure of a 70S ribosome-tRNA complex reveals functional interactions and rearrangements. Cell 126: 1065-1077.
    • (2006) Cell , vol.126 , pp. 1065-1077
    • Korostelev, A.1    Trakhanov, S.2    Laurberg, M.3    Noler, H.F.4
  • 19
    • 0023216779 scopus 로고
    • In vitro synthesis of 16S ribosomal RNA containing single base changes and assembly into a functional 30S ribosome
    • Krzyzosiak, W., Denman, R., Nurse, K., Hellmann, W., Boublik, M., Gehrke, C.W., Agris, T.F., and Ofengand, J. 1987. In vitro synthesis of 16S ribosomal RNA containing single base changes and assembly into a functional 30S ribosome. Biochemistry 26: 2353-2364.
    • (1987) Biochemistry , vol.26 , pp. 2353-2364
    • Krzyzosiak, W.1    Denman, R.2    Nurse, K.3    Hellmann, W.4    Boublik, M.5    Gehrke, C.W.6    Agris, T.F.7    Ofengand, J.8
  • 21
    • 0016607629 scopus 로고
    • Intermediates and time kinetics of the in vivo assembly of Escherichia coli ribosomes
    • Lindhal, L. 1975. Intermediates and time kinetics of the in vivo assembly of Escherichia coli ribosomes. J. Mol. Biol. 92: 15-37.
    • (1975) J. Mol. Biol , vol.92 , pp. 15-37
    • Lindhal, L.1
  • 22
    • 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
    • doi: 10.1093/nar/gkg666
    • Maravic, G., Bujnicki, J.M., Feder, M., Pongor, S., and Flögel, M. 2003. 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: 4941-4949. doi: 10.1093/nar/gkg666.
    • (2003) Nucleic Acids Res , vol.31 , pp. 4941-4949
    • Maravic, G.1    Bujnicki, J.M.2    Feder, M.3    Pongor, S.4    Flögel, M.5
  • 24
    • 0035721651 scopus 로고    scopus 로고
    • Mapping pseudouridines in RNA molecules
    • Ofengand, J., Del Campo, M., and Kaya, Y. 2001. Mapping pseudouridines in RNA molecules. Methods 25: 365-373.
    • (2001) Methods , vol.25 , pp. 365-373
    • Ofengand, J.1    Del Campo, M.2    Kaya, Y.3
  • 25
    • 33846678393 scopus 로고    scopus 로고
    • Loss of a conserved 7-methylguanosine modification in 16S rRNA confers low-level streptomycin resistance in bacteria
    • Okamoto, S., Tamaru, A., Nakajima, C., Nishimura, K., Tanaka, Y., Tokoyuma, S., Suzuki, Y., and Ochi, K. 2007. Loss of a conserved 7-methylguanosine modification in 16S rRNA confers low-level streptomycin resistance in bacteria. Mol. Microbiol. 63: 1096-1106.
    • (2007) Mol. Microbiol , vol.63 , pp. 1096-1106
    • Okamoto, S.1    Tamaru, A.2    Nakajima, C.3    Nishimura, K.4    Tanaka, Y.5    Tokoyuma, S.6    Suzuki, Y.7    Ochi, K.8
  • 26
    • 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. 1979. 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: 9094-9100.
    • (1979) J. Biol. Chem , vol.254 , pp. 9094-9100
    • Poldermans, B.1    Roza, L.2    Van Knippenberg, P.H.3
  • 27
    • 0027171312 scopus 로고
    • Dynamics of in vitro assembly of 16 S rRNA into 30 S ribosomal subunits
    • Powers, T., Daubresse, G., and Noller, H.F. 1993. Dynamics of in vitro assembly of 16 S rRNA into 30 S ribosomal subunits. J. Mol. Biol. 232: 362-374.
    • (1993) J. Mol. Biol , vol.232 , pp. 362-374
    • Powers, T.1    Daubresse, G.2    Noller, H.F.3
  • 31
    • 15144342115 scopus 로고
    • Interconversions between inactive and active forms of ribosomal subunits
    • Zamir, A., Miskin, R., and Elson, D. 1969. Interconversions between inactive and active forms of ribosomal subunits. FEBS Lett. 3: 85-88.
    • (1969) FEBS Lett , vol.3 , pp. 85-88
    • Zamir, A.1    Miskin, R.2    Elson, D.3
  • 32
    • 0015223366 scopus 로고
    • Inactivation and reactivation of ribosomal subunits: Amino acyl-transfer RNA binding activity of the 30 s subunit of Escherichia coli
    • Zamir, A., Miskin, R., and Elson, D. 1971. Inactivation and reactivation of ribosomal subunits: Amino acyl-transfer RNA binding activity of the 30 s subunit of Escherichia coli. J. Mol. Biol. 60: 347-364.
    • (1971) J. Mol. Biol , vol.60 , pp. 347-364
    • Zamir, A.1    Miskin, R.2    Elson, D.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.