메뉴 건너뛰기




Volumn 33, Issue 16, 2005, Pages 5291-5296

Deacylated tRNA is released from the E site upon A site occupation but before GTP is hydrolyzed by EF-Tu

Author keywords

[No Author keywords available]

Indexed keywords

AMINOACYL TRANSFER RNA; ELONGATION FACTOR TU; GUANOSINE TRIPHOSPHATE; PEPTIDYLTRANSFERASE; PUROMYCIN; RIBOSOME RNA; TRANSFER RNA;

EID: 24944586007     PISSN: 03051048     EISSN: 13624962     Source Type: Journal    
DOI: 10.1093/nar/gki833     Document Type: Article
Times cited : (36)

References (19)
  • 1
    • 0025280137 scopus 로고
    • The allosteric three-site model for the ribosomal elongation cycle: Features and future
    • Nierhaus,K.H. (1990) The allosteric three-site model for the ribosomal elongation cycle: Features and future. Biochemistry, 29, 4997-5008.
    • (1990) Biochemistry , vol.29 , pp. 4997-5008
    • Nierhaus, K.H.1
  • 2
    • 0020554836 scopus 로고
    • Testing an alternative model for the ribosomal peptide elongation cycle
    • Rheinberger,H.-J. and Nierhaus,K.H. (1983) Testing an alternative model for the ribosomal peptide elongation cycle. Proc. Natl Acad. Sci. USA, 80, 4213-4217.
    • (1983) Proc. Natl. Acad. Sci. USA , vol.80 , pp. 4213-4217
    • Rheinberger, H.-J.1    Nierhaus, K.H.2
  • 3
    • 1642564526 scopus 로고    scopus 로고
    • Dissecting the ribosomal inhibition mechanisms of edeine and pactamycin: The universally conserved residues G693 and C795 regulate P-site tRNA binding
    • Dinos,G., Wilson,D.N., Teraoka,Y., Szaflarski,W., Fucini,P., Kalpaxis,D. and Nierhaus,K.H. (2004) Dissecting the ribosomal inhibition mechanisms of edeine and pactamycin: The universally conserved residues G693 and C795 regulate P-site tRNA binding. Mol. Cell, 13, 113-124.
    • (2004) Mol. Cell , vol.13 , pp. 113-124
    • Dinos, G.1    Wilson, D.N.2    Teraoka, Y.3    Szaflarski, W.4    Fucini, P.5    Kalpaxis, D.6    Nierhaus, K.H.7
  • 4
    • 0026783192 scopus 로고
    • Kinetic and thermodynamic parameters for transfer RNA binding to the ribosome and for the translocation reaction
    • Schilling-Bartetzko,S., Bartetzko,A. and Nierhaus,K.H. (1992) Kinetic and thermodynamic parameters for transfer RNA binding to the ribosome and for the translocation reaction. J. Biol. Chem., 267, 4703-4712.
    • (1992) J. Biol. Chem. , vol.267 , pp. 4703-4712
    • Schilling-Bartetzko, S.1    Bartetzko, A.2    Nierhaus, K.H.3
  • 5
    • 0242414021 scopus 로고    scopus 로고
    • A functional interaction between ribosomal proteins S7 and S11 within the bacterial ribosome
    • Robert,F. and Brakier-Gingras,L. (2003) A functional interaction between ribosomal proteins S7 and S11 within the bacterial ribosome. J. Biol. Chem., 278, 44913-44920.
    • (2003) J. Biol. Chem. , vol.278 , pp. 44913-44920
    • Robert, F.1    Brakier-Gingras, L.2
  • 6
    • 1942533456 scopus 로고    scopus 로고
    • tRNA slippage at the tmRNA resume codon
    • Trimble,M.J., Minnicus,A. and Williams,K.P. (2004) tRNA slippage at the tmRNA resume codon. RNA, 10, 805-812.
    • (2004) RNA , vol.10 , pp. 805-812
    • Trimble, M.J.1    Minnicus, A.2    Williams, K.P.3
  • 7
    • 3142562521 scopus 로고    scopus 로고
    • Maintaining the ribosomal reading frame: The influence of the E site during translational regulation of release factor 2
    • Marquez,V., Wilson,D.N., Tate,W.P., Triana-Alonso,F. and Nierhaus,K.H. (2004) Maintaining the ribosomal reading frame: The influence of the E site during translational regulation of release factor 2. Cell, 118, 45-55.
    • (2004) Cell , vol.118 , pp. 45-55
    • Marquez, V.1    Wilson, D.N.2    Tate, W.P.3    Triana-Alonso, F.4    Nierhaus, K.H.5
  • 9
    • 0036384314 scopus 로고    scopus 로고
    • The protein synthesis inhibitors, oxazolidinones and chloramphenicol, cause extensive translational inaccuracy in vivo
    • Thompson,J., O'Connor,M., Mills,J.A. and Dahlberg,A.E. (2002) The protein synthesis inhibitors, oxazolidinones and chloramphenicol, cause extensive translational inaccuracy in vivo. J. Mol. Biol., 322, 273-279.
    • (2002) J. Mol. Biol. , vol.322 , pp. 273-279
    • Thompson, J.1    O'Connor, M.2    Mills, J.A.3    Dahlberg, A.E.4
  • 10
    • 0034086680 scopus 로고    scopus 로고
    • Preparation of functional ribosomal complexes and the effect of buffer conditions on tRNA positions observed by cryoelectron microscopy
    • Blaha,G., Stelzl,U., Spahn,C.M.T., Agrawal,R.K., Frank,J. and Nierhaus,K.H. (2000) Preparation of functional ribosomal complexes and the effect of buffer conditions on tRNA positions observed by cryoelectron microscopy. Methods Enzymol., 317, 292-309.
    • (2000) Methods Enzymol. , vol.317 , pp. 292-309
    • Blaha, G.1    Stelzl, U.2    Spahn, C.M.T.3    Agrawal, R.K.4    Frank, J.5    Nierhaus, K.H.6
  • 11
    • 0037166262 scopus 로고    scopus 로고
    • Codon anticodon interaction at the P Site is a prerequisite for tRNA interaction with the small ribosomal subunit
    • Schäfer,M.A., Tastan,A.O., Patzke,S., Blaha,G., Spahn,C.M., Wilson,D.N. and Nierhaus,K.H. (2002) Codon anticodon interaction at the P Site is a prerequisite for tRNA interaction with the small ribosomal subunit. J. Biol. Chem., 277, 19095-19105.
    • (2002) J. Biol. Chem. , vol.277 , pp. 19095-19105
    • Schäfer, M.A.1    Tastan, A.O.2    Patzke, S.3    Blaha, G.4    Spahn, C.M.5    Wilson, D.N.6    Nierhaus, K.H.7
  • 12
    • 0029959815 scopus 로고    scopus 로고
    • The 'allosteric three-site model' of elongation cannot be confirmed in a well-defined ribosome system from Escherichia coli
    • Semenkov,Y.P., Rodnina,M.V. and Wintermeyer,W. (1996) The 'allosteric three-site model' of elongation cannot be confirmed in a well-defined ribosome system from Escherichia coli. Proc. Natl Acad. Sci. USA, 93, 12183-12188.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 12183-12188
    • Semenkov, Y.P.1    Rodnina, M.V.2    Wintermeyer, W.3
  • 13
    • 0024411663 scopus 로고
    • The third ribosomal tRNA-binding site, the E site, is occupied in native polysomes
    • Remme,J., Margus,T., Villems,R. and Nierhaus,K.H. (1989) The third ribosomal tRNA-binding site, the E site, is occupied in native polysomes. Eur. J. Biochem., 183, 281-284.
    • (1989) Eur. J. Biochem. , vol.183 , pp. 281-284
    • Remme, J.1    Margus, T.2    Villems, R.3    Nierhaus, K.H.4
  • 14
    • 2542564300 scopus 로고    scopus 로고
    • The ribosome as an entropy trap
    • [Erratum (2004) Proc. Natl Acad. Sci. USA, 101, 12397-12398.]
    • Sievers,A., Beringer,M., Rodnina,M.V. and Wolfenden,R. (2004) The ribosome as an entropy trap [Erratum (2004) Proc. Natl Acad. Sci. USA, 101, 12397-12398.]. Proc. Natl Acad. Sci. USA, 101, 7897-7901.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 7897-7901
    • Sievers, A.1    Beringer, M.2    Rodnina, M.V.3    Wolfenden, R.4
  • 17
    • 2542470615 scopus 로고    scopus 로고
    • The active site of the ribosome is composed of two layers of conserved nucleotides with distinct roles in peptide bond formation and peptide release
    • Youngman,E.M., Brunelle,J.L., Kochaniak,A.B. and Green,R. (2004) The active site of the ribosome is composed of two layers of conserved nucleotides with distinct roles in peptide bond formation and peptide release. Cell, 117, 589-599.
    • (2004) Cell , vol.117 , pp. 589-599
    • Youngman, E.M.1    Brunelle, J.L.2    Kochaniak, A.B.3    Green, R.4
  • 18
    • 1342302787 scopus 로고    scopus 로고
    • Dial tm for rescue: tmRNA engages ribosomes stalled on defective mRNAs
    • Haebel,P.W., Gutmann,S. and Ban,N. (2004) Dial tm for rescue: TmRNA engages ribosomes stalled on defective mRNAs. Curr. Opin. Struct. Biol., 14, 58-65.
    • (2004) Curr. Opin. Struct. Biol. , vol.14 , pp. 58-65
    • Haebel, P.W.1    Gutmann, S.2    Ban, N.3
  • 19
    • 17844381357 scopus 로고    scopus 로고
    • Independent binding sites of small protein B onto transfer-messenger RNA during trans-translation
    • Metzinger,L., Hallier,M. and Felden,B. (2005) Independent binding sites of small protein B onto transfer-messenger RNA during trans-translation. Nucleic Acids Res., 33, 2384-2394.
    • (2005) Nucleic Acids Res. , vol.33 , pp. 2384-2394
    • Metzinger, L.1    Hallier, M.2    Felden, B.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.