메뉴 건너뛰기




Volumn 15, Issue 2, 2009, Pages 346-354

Synthesis and functional activity of tRNAs labeled with fluorescent hydrazides in the D-loop

Author keywords

Cy3; Cy5; Dihydrouridine; FRET; Hydrazide; Translocation; tRNA

Indexed keywords

HYDRAZIDE DERIVATIVE; TRANSFER RNA;

EID: 58249096649     PISSN: 13558382     EISSN: 14699001     Source Type: Journal    
DOI: 10.1261/rna.1257509     Document Type: Article
Times cited : (48)

References (31)
  • 2
    • 33745071762 scopus 로고    scopus 로고
    • Peptide bond formation does not involve acid-base catalysis by ribosomal residues
    • Bieling, P., Beringer, M., Adio, S., and Rodnina, M.V. 2006. Peptide bond formation does not involve acid-base catalysis by ribosomal residues. Nat. Struct. Mol. Biol. 13: 423-428.
    • (2006) Nat. Struct. Mol. Biol , vol.13 , pp. 423-428
    • Bieling, P.1    Beringer, M.2    Adio, S.3    Rodnina, M.V.4
  • 5
    • 0014219460 scopus 로고
    • Selective reduction of yeast transfer ribonucleic acid with sodium borohydride
    • Cerutti, P. and Miller, N. 1967. Selective reduction of yeast transfer ribonucleic acid with sodium borohydride. J. Mol. Biol. 26: 55-66.
    • (1967) J. Mol. Biol , vol.26 , pp. 55-66
    • Cerutti, P.1    Miller, N.2
  • 6
    • 0000352887 scopus 로고
    • On the mechanism of Schiff base formation and hydrolysis
    • Cordes, E.H. and Jencks, W.P. 1962. On the mechanism of Schiff base formation and hydrolysis. J. Am. Chem. Soc. 84: 832-837.
    • (1962) J. Am. Chem. Soc , vol.84 , pp. 832-837
    • Cordes, E.H.1    Jencks, W.P.2
  • 7
    • 42949126723 scopus 로고    scopus 로고
    • Coupling of ribosomal L1 stalk and tRNA dynamics during translation elongation
    • Fei, J., Kosuri, P., MacDougall, D.D., and Gonzalez Jr., R.L. 2008. Coupling of ribosomal L1 stalk and tRNA dynamics during translation elongation. Mol. Cell 30: 348-359.
    • (2008) Mol. Cell , vol.30 , pp. 348-359
    • Fei, J.1    Kosuri, P.2    MacDougall, D.D.3    Gonzalez Jr., R.L.4
  • 8
    • 34748843156 scopus 로고    scopus 로고
    • A quantitative kinetic scheme for 70 S translation initiation complex formation
    • Grigoriadou, C., Marzi, S., Kirillov, S., Gualerzi, C.O., and Cooperman, B.S. 2007a. A quantitative kinetic scheme for 70 S translation initiation complex formation. J. Mol. Biol. 373: 562-572.
    • (2007) J. Mol. Biol , vol.373 , pp. 562-572
    • Grigoriadou, C.1    Marzi, S.2    Kirillov, S.3    Gualerzi, C.O.4    Cooperman, B.S.5
  • 9
    • 34748909381 scopus 로고    scopus 로고
    • The translational fidelity function of IF3 during transition from the 30 S initiation complex to the 70 S initiation complex
    • Grigoriadou, C., Marzi, S., Pan, D., Gualerzi, C.O., and Cooperman, B.S. 2007b. The translational fidelity function of IF3 during transition from the 30 S initiation complex to the 70 S initiation complex. J. Mol. Biol. 373: 551-561.
    • (2007) J. Mol. Biol , vol.373 , pp. 551-561
    • Grigoriadou, C.1    Marzi, S.2    Pan, D.3    Gualerzi, C.O.4    Cooperman, B.S.5
  • 10
    • 85050903073 scopus 로고
    • Mechanism and catalysis of simple carbonyl group reactions
    • Jencks, W.P. 1964. Mechanism and catalysis of simple carbonyl group reactions. Prog. Phys. Org. Chem. 2: 63-128.
    • (1964) Prog. Phys. Org. Chem , vol.2 , pp. 63-128
    • Jencks, W.P.1
  • 11
    • 33845995459 scopus 로고    scopus 로고
    • Ala with modified uridine in the wobble position
    • Ala with modified uridine in the wobble position. Mol. Cell 25: 167-174.
    • (2007) Mol. Cell , vol.25 , pp. 167-174
    • Kothe, U.1    Rodnina, M.V.2
  • 13
    • 38049103060 scopus 로고    scopus 로고
    • Controlled release of volatile aldehydes and ketones from dynamic mixtures generated by reversible hydrazone formation
    • Levrand, B., Fieber, W., Lehn, J.-M., and Herrmann, A. 2007. Controlled release of volatile aldehydes and ketones from dynamic mixtures generated by reversible hydrazone formation. Helv. Chim. Acta 90: 2281-2314.
    • (2007) Helv. Chim. Acta , vol.90 , pp. 2281-2314
    • Levrand, B.1    Fieber, W.2    Lehn, J.-M.3    Herrmann, A.4
  • 15
    • 33847051154 scopus 로고    scopus 로고
    • Identification of two distinct hybrid state intermediates on the ribosome
    • Munro, J.B., Altman, R.B., O'Connor, N., and Blanchard, S.C. 2007. Identification of two distinct hybrid state intermediates on the ribosome. Mol. Cell 25: 505-517.
    • (2007) Mol. Cell , vol.25 , pp. 505-517
    • Munro, J.B.1    Altman, R.B.2    O'Connor, N.3    Blanchard, S.C.4
  • 16
    • 33745044746 scopus 로고    scopus 로고
    • Rapid ribosomal translocation depends on the conserved 18-55 base pair in P-site transfer RNA
    • Pan, D., Kirillov, S., Zhang, C.M., Hou, Y.M., and Cooperman, B.S. 2006. Rapid ribosomal translocation depends on the conserved 18-55 base pair in P-site transfer RNA. Nat. Struct. Mol. Biol. 13: 354-359.
    • (2006) Nat. Struct. Mol. Biol , vol.13 , pp. 354-359
    • Pan, D.1    Kirillov, S.2    Zhang, C.M.3    Hou, Y.M.4    Cooperman, B.S.5
  • 17
    • 33847024820 scopus 로고    scopus 로고
    • Kinetically competent intermediates in the translocation step of protein synthesis
    • Pan, D., Kirillov, S.V., and Cooperman, B.S. 2007. Kinetically competent intermediates in the translocation step of protein synthesis. Mol. Cell 25: 519-529.
    • (2007) Mol. Cell , vol.25 , pp. 519-529
    • Pan, D.1    Kirillov, S.V.2    Cooperman, B.S.3
  • 18
    • 49649091161 scopus 로고    scopus 로고
    • Perturbation of the tRNA tertiary core differentially affects specific steps of the elongation cycle
    • Pan, D., Zhang, C.M., Kirillov, S., Hou, Y.M., and Cooperman, B.S. 2008. Perturbation of the tRNA tertiary core differentially affects specific steps of the elongation cycle. J. Biol. Chem. 283: 18431-18440.
    • (2008) J. Biol. Chem , vol.283 , pp. 18431-18440
    • Pan, D.1    Zhang, C.M.2    Kirillov, S.3    Hou, Y.M.4    Cooperman, B.S.5
  • 19
    • 0032535207 scopus 로고    scopus 로고
    • Complete kinetic mechanism of elongation factor Tu-dependent binding of aminoacyl-tRNA to the A site of the E. coli ribosome
    • Pape, T., Wintermeyer, W., and Rodnina, M.V. 1998. Complete kinetic mechanism of elongation factor Tu-dependent binding of aminoacyl-tRNA to the A site of the E. coli ribosome. EMBO J. 17: 7490-7497.
    • (1998) EMBO J , vol.17 , pp. 7490-7497
    • Pape, T.1    Wintermeyer, W.2    Rodnina, M.V.3
  • 20
    • 0028109919 scopus 로고
    • Transient conformational states of aminoacyl-tRNA during ribosome binding catalyzed by elongation factor Tu
    • Rodnina, M.V., Fricke, R., and Wintermeyer, W. 1994. Transient conformational states of aminoacyl-tRNA during ribosome binding catalyzed by elongation factor Tu. Biochemistry 33: 12267-12275.
    • (1994) Biochemistry , vol.33 , pp. 12267-12275
    • Rodnina, M.V.1    Fricke, R.2    Wintermeyer, W.3
  • 21
    • 0031028688 scopus 로고    scopus 로고
    • Hydrolysis of GTP by elongation factor G drives tRNA movement on the ribosome
    • Rodnina, M.V., Savelsbergh, A., Katunin, V.I., and Wintermeyer, W. 1997. Hydrolysis of GTP by elongation factor G drives tRNA movement on the ribosome. Nature 385: 37-41.
    • (1997) Nature , vol.385 , pp. 37-41
    • Rodnina, M.V.1    Savelsbergh, A.2    Katunin, V.I.3    Wintermeyer, W.4
  • 22
    • 0038433302 scopus 로고    scopus 로고
    • An elongation factor G-induced ribosome rearrangement precedes tRNA-mRNA translocation
    • Savelsbergh, A., Katunin, V.I., Mohr, D., Peske, F., Rodnina, M.V., and Wintermeyer, W. 2003. An elongation factor G-induced ribosome rearrangement precedes tRNA-mRNA translocation. Mol. Cell 11: 1517-1523.
    • (2003) Mol. Cell , vol.11 , pp. 1517-1523
    • Savelsbergh, A.1    Katunin, V.I.2    Mohr, D.3    Peske, F.4    Rodnina, M.V.5    Wintermeyer, W.6
  • 24
    • 0014428762 scopus 로고
    • A specific modification next to the anticodon of phenylalanine transfer ribonucleic acid
    • Thiebe, R. and Zachau, H.G. 1968. A specific modification next to the anticodon of phenylalanine transfer ribonucleic acid. Eur. J. Biochem. 5: 546-555.
    • (1968) Eur. J. Biochem , vol.5 , pp. 546-555
    • Thiebe, R.1    Zachau, H.G.2
  • 25
    • 49649150311 scopus 로고
    • Replacement of Y base, dihydrouracil, and 7-methylguanine in tRNA by artificial odd bases
    • Wintermeyer, W. and Zachau, H.G. 1971. Replacement of Y base, dihydrouracil, and 7-methylguanine in tRNA by artificial odd bases. FEBS Lett. 18: 214-218.
    • (1971) FEBS Lett , vol.18 , pp. 214-218
    • Wintermeyer, W.1    Zachau, H.G.2
  • 26
    • 0016023632 scopus 로고
    • Replacement of odd bases in tRNA by fluorescent dyes
    • Wintermeyer, W. and Zachau, H.G. 1974. Replacement of odd bases in tRNA by fluorescent dyes. Methods Enzymol. 29: 667-673.
    • (1974) Methods Enzymol , vol.29 , pp. 667-673
    • Wintermeyer, W.1    Zachau, H.G.2
  • 28
    • 0018338913 scopus 로고
    • Incorporation of amines or hydrazines into tRNA replacing wybutine or dihydrouracil
    • Wintermeyer, W., Schleich, H.G., and Zachau, H.G. 1979. Incorporation of amines or hydrazines into tRNA replacing wybutine or dihydrouracil. Methods Enzymol. 59: 110-121.
    • (1979) Methods Enzymol , vol.59 , pp. 110-121
    • Wintermeyer, W.1    Schleich, H.G.2    Zachau, H.G.3
  • 29
    • 1542358892 scopus 로고    scopus 로고
    • Nascent membrane and secretory proteins differ in FRET-detected folding far inside the ribosome and in their exposure to ribosomal proteins
    • Woolhead, C.A., McCormick, P.J., and Johnson, A.E. 2004. Nascent membrane and secretory proteins differ in FRET-detected folding far inside the ribosome and in their exposure to ribosomal proteins. Cell 116: 725-736.
    • (2004) Cell , vol.116 , pp. 725-736
    • Woolhead, C.A.1    McCormick, P.J.2    Johnson, A.E.3
  • 30
    • 0003932366 scopus 로고
    • Studies of transfer RNA tertiary structure of singlet-singlet energy transfer
    • Yang, C.H. and Söll, D. 1974. Studies of transfer RNA tertiary structure of singlet-singlet energy transfer. Proc. Natl. Acad. Sci. 71: 2838-2842.
    • (1974) Proc. Natl. Acad. Sci , vol.71 , pp. 2838-2842
    • Yang, C.H.1    Söll, D.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.