메뉴 건너뛰기




Volumn 29, Issue 2, 1998, Pages 409-417

Initiation factors of protein biosynthesis in bacteria and their structural relationship to elongation and termination factors

Author keywords

[No Author keywords available]

Indexed keywords

ELONGATION FACTOR; ELONGATION FACTOR G; ELONGATION FACTOR TU; INITIATION FACTOR 1; INITIATION FACTOR 2; INITIATION FACTOR 3; MESSENGER RNA; RIBOSOME PROTEIN;

EID: 0031854151     PISSN: 0950382X     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1365-2958.1998.00893.x     Document Type: Review
Times cited : (65)

References (34)
  • 1
    • 0030584663 scopus 로고    scopus 로고
    • A complex profile of protein elongation: Translating chemical energy into molecular movement
    • Abel, K., and Jurnak, F. (1996) A complex profile of protein elongation: translating chemical energy into molecular movement. Structure 4: 229-238.
    • (1996) Structure , vol.4 , pp. 229-238
    • Abel, K.1    Jurnak, F.2
  • 2
    • 0029563262 scopus 로고
    • Structure-based sequence alignment of elongation factors Tu and G with related GTPases involved in translation
    • AEvarsson, A. (1995) Structure-based sequence alignment of elongation factors Tu and G with related GTPases involved in translation. J Mol Evol 41: 1096-1104.
    • (1995) J Mol Evol , vol.41 , pp. 1096-1104
    • AEvarsson, A.1
  • 3
    • 0028059544 scopus 로고
    • Three-dimensional structure of the ribosomal translocase: Elongation factor G from Thermus thermophilus
    • AEvarsson, A., Brazhnikov, E., Garber, M., Zheltonosova, J., Chirgadze, Y., Al-Karadaghi, et al. (1994) Three-dimensional structure of the ribosomal translocase: elongation factor G from Thermus thermophilus. EMBO J 13: 3669-3677.
    • (1994) EMBO J , vol.13 , pp. 3669-3677
    • AEvarsson, A.1    Brazhnikov, E.2    Garber, M.3    Zheltonosova, J.4    Chirgadze, Y.5    Al-Karadaghi6
  • 4
    • 0029111710 scopus 로고
    • X-ray crystallography shows that translational initiation factor IF3 consists of two compact α/β domains linked by an α-helix
    • Biou, V., Shu, F., and Ramakrishnan, V. (1995) X-ray crystallography shows that translational initiation factor IF3 consists of two compact α/β domains linked by an α-helix. EMBO J 14: 4056-4064.
    • (1995) EMBO J , vol.14 , pp. 4056-4064
    • Biou, V.1    Shu, F.2    Ramakrishnan, V.3
  • 5
    • 0021109418 scopus 로고
    • Direct cross-links between initiation factors 1, 2, and 3 and ribosomal proteins promoted by 2-iminothiolane
    • Boileau, G., Butler, P., Hershey, J.W.B., and Traut, R.R. (1983) Direct cross-links between initiation factors 1, 2, and 3 and ribosomal proteins promoted by 2-iminothiolane. Biochemistry 22: 3162-3170.
    • (1983) Biochemistry , vol.22 , pp. 3162-3170
    • Boileau, G.1    Butler, P.2    Hershey, J.W.B.3    Traut, R.R.4
  • 6
    • 0027980558 scopus 로고
    • The crystal structure of elongation factor G complexed with GDP, at 2.7 Å resolution
    • Czworkowski, J., Wang, J., Steitz, T.A., and Moore, P.B. (1994) The crystal structure of elongation factor G complexed with GDP, at 2.7 Å resolution. EMBO J 13: 3661-3668.
    • (1994) EMBO J , vol.13 , pp. 3661-3668
    • Czworkowski, J.1    Wang, J.2    Steitz, T.A.3    Moore, P.B.4
  • 7
    • 0029100747 scopus 로고
    • A model for protein synthesis based on cryo-electron microscopy of the E. coli ribosome
    • Frank, J., Zhu, J., Penczek, P., Li, Y., Srivastava, S., Verschoor, A., et al. (1995) A model for protein synthesis based on cryo-electron microscopy of the E. coli ribosome. Nature 376: 441-444.
    • (1995) Nature , vol.376 , pp. 441-444
    • Frank, J.1    Zhu, J.2    Penczek, P.3    Li, Y.4    Srivastava, S.5    Verschoor, A.6
  • 9
    • 0030970289 scopus 로고    scopus 로고
    • Ribosomes and translation
    • Green, R., and Noller, H.F. (1997) Ribosomes and translation. Annu Rev Biochem 66: 679-716.
    • (1997) Annu Rev Biochem , vol.66 , pp. 679-716
    • Green, R.1    Noller, H.F.2
  • 10
    • 0025365804 scopus 로고
    • Initiation of mRNA translation in prokaryotes
    • Gualerzi, C.O., and Pon, C.L (1990) Initiation of mRNA translation in prokaryotes. Biochemistry 29: 5881-5889.
    • (1990) Biochemistry , vol.29 , pp. 5881-5889
    • Gualerzi, C.O.1    Pon, C.L.2
  • 11
    • 0024835265 scopus 로고
    • Selection of the initiator tRNA by Escherichia coli initiation factors
    • Hartz, D., McPheeters, D.S., and Gold, L. (1989) Selection of the initiator tRNA by Escherichia coli initiation factors. Genes Dev 3: 1899-1912.
    • (1989) Genes Dev , vol.3 , pp. 1899-1912
    • Hartz, D.1    McPheeters, D.S.2    Gold, L.3
  • 12
    • 0017035617 scopus 로고
    • Cross-linking of initiation factor IF2 to proteins L7/L12 in 70S ribosomes of Escherichia coli
    • Heimark, R.L., Hershey, J.W.B., and Traut, R.R. (1976) Cross-linking of initiation factor IF2 to proteins L7/L12 in 70S ribosomes of Escherichia coli. J Biol Chem 251: 7779-7784.
    • (1976) J Biol Chem , vol.251 , pp. 7779-7784
    • Heimark, R.L.1    Hershey, J.W.B.2    Traut, R.R.3
  • 13
    • 0029975504 scopus 로고    scopus 로고
    • Conserved motifs in prokaryotic and eukaryotic polypeptide release factors: tRNA-protein mimicry hypothesis
    • Ito, K., Ebihara, K., Uno, M., and Nakamura, Y. (1996) Conserved motifs in prokaryotic and eukaryotic polypeptide release factors: tRNA-protein mimicry hypothesis. Proc Natl Acad Sci USA 93: 5443-5448.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 5443-5448
    • Ito, K.1    Ebihara, K.2    Uno, M.3    Nakamura, Y.4
  • 14
    • 0029913289 scopus 로고    scopus 로고
    • Late events in translation initiation. Adjustment of fMet-tRNA in the ribosomal P site
    • La Teana, A., Pon, C.L, and Gualerzi, C.O. (1996) Late events in translation initiation. Adjustment of fMet-tRNA in the ribosomal P site. J Mol Biol 256: 667-675.
    • (1996) J Mol Biol , vol.256 , pp. 667-675
    • La Teana, A.1    Pon, C.L.2    Gualerzi, C.O.3
  • 15
    • 0026655170 scopus 로고
    • How are tRNAs and mRNA arranged in the ribosome? An attempt to correlate the stereochemistry of the tRNA-mRNA interaction with constraints imposed by the ribosomal topography
    • Lim, V., Venclovas, C., Spirin, A., Brimacombe, R., Mitchell, P., and Müller, F. (1992) How are tRNAs and mRNA arranged in the ribosome? An attempt to correlate the stereochemistry of the tRNA-mRNA interaction with constraints imposed by the ribosomal topography. Nucleic Acids Res 20: 2627-2637.
    • (1992) Nucleic Acids Res , vol.20 , pp. 2627-2637
    • Lim, V.1    Venclovas, C.2    Spirin, A.3    Brimacombe, R.4    Mitchell, P.5    Müller, F.6
  • 16
    • 0030899747 scopus 로고    scopus 로고
    • Translational initiation factor IF2 from Bacillus stearothermophilus: A spectroscopic and microcalorimetric study of the C-domain
    • Misselwitz, R., Welfle, K., Krafft, C., Gualerzi, C.O., and Welfe, H. (1997) Translational initiation factor IF2 from Bacillus stearothermophilus: a spectroscopic and microcalorimetric study of the C-domain. Biochemistry 36: 3170-3178.
    • (1997) Biochemistry , vol.36 , pp. 3170-3178
    • Misselwitz, R.1    Welfle, K.2    Krafft, C.3    Gualerzi, C.O.4    Welfe, H.5
  • 17
    • 0029051704 scopus 로고
    • Specific protection of 16S RNA by translational initiation factors
    • Moazed, D., Samaha, R.R., Gualerzi, C., and Noller, H.F. (1995) Specific protection of 16S RNA by translational initiation factors. J Mol Biol 248: 207-210.
    • (1995) J Mol Biol , vol.248 , pp. 207-210
    • Moazed, D.1    Samaha, R.R.2    Gualerzi, C.3    Noller, H.F.4
  • 18
    • 0031566955 scopus 로고    scopus 로고
    • Heteronuclear NMR studies of E.coli translation initiation factor IF3. Evidence that the inter-domain region is disordered in solution
    • Moreau, M., deCock, E., Fortier, P.-L., Garcia, C., Albaret, C., Blanquet, S., et al. (1997) Heteronuclear NMR studies of E.coli translation initiation factor IF3. Evidence that the inter-domain region is disordered in solution. J Mol Biol 266: 15-22.
    • (1997) J Mol Biol , vol.266 , pp. 15-22
    • Moreau, M.1    DeCock, E.2    Fortier, P.-L.3    Garcia, C.4    Albaret, C.5    Blanquet, S.6
  • 19
    • 0030592511 scopus 로고    scopus 로고
    • Emerging understanding of translation termination
    • Nakamura, Y., Ito, K., and lsaksson, L.A. (1996) Emerging understanding of translation termination. Cell 87: 147-150.
    • (1996) Cell , vol.87 , pp. 147-150
    • Nakamura, Y.1    Ito, K.2    Lsaksson, L.A.3
  • 23
    • 0002084108 scopus 로고
    • Initiator tRNAs and initiation of protein synthesis
    • Söll, D., and RajBhandary, U. (eds). Washington, DC: American Society for Microbiology
    • RajBhandary, U.L., and Chow, C.M. (1995) Initiator tRNAs and initiation of protein synthesis. In tRNA: Structure, Biosynthesis, and Function. Söll, D., and RajBhandary, U. (eds). Washington, DC: American Society for Microbiology, pp. 511-527.
    • (1995) tRNA: Structure, Biosynthesis, and Function , pp. 511-527
    • RajBhandary, U.L.1    Chow, C.M.2
  • 24
    • 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.L., 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.L.3    Wintermeyer, W.4
  • 25
    • 0031002350 scopus 로고    scopus 로고
    • The structure of the translational initiation factor IF1 from E. coli contains an oligomer-binding motif
    • Sette, M., van Tilborg, P., Spurio, R., Kaptein, R., Paci, M., Gualerzi, C.O., and Boelens, R. (1997) The structure of the translational initiation factor IF1 from E. coli contains an oligomer-binding motif. EMBO J 16: 1436-1443.
    • (1997) EMBO J , vol.16 , pp. 1436-1443
    • Sette, M.1    Van Tilborg, P.2    Spurio, R.3    Kaptein, R.4    Paci, M.5    Gualerzi, C.O.6    Boelens, R.7
  • 26
    • 0002165127 scopus 로고
    • Novel structural and functional aspects of translational initiation factor IF2
    • Nierhaus, K.H., Franceschi, F., Subramanian, A.R., Erdmann, V.A., and Wittmann-Liebold, B. (eds). New York: Plenum Press
    • Spurio, R., Severini, M., La Teana, A., Canonaco, M.A., Pawlik, R.T., Gualerzi, C.O., and Pon, C.L. (1993) Novel structural and functional aspects of translational initiation factor IF2. In The Translational Apparatus: Structure, Function, Regulation and Evolution. Nierhaus, K.H., Franceschi, F., Subramanian, A.R., Erdmann, V.A., and Wittmann-Liebold, B. (eds). New York: Plenum Press, pp. 241-252.
    • (1993) The Translational Apparatus: Structure, Function, Regulation and Evolution , pp. 241-252
    • Spurio, R.1    Severini, M.2    La Teana, A.3    Canonaco, M.A.4    Pawlik, R.T.5    Gualerzi, C.O.6    Pon, C.L.7
  • 27
    • 0029645318 scopus 로고
    • The 70S Escherichia coli ribosome at 23 Å resolution: Fitting the ribosomal RNA
    • Stark, H., Mueller, F., Orlova, E.V., Schatz, M., Dube, P., Erdemir, T., et al. (1995) The 70S Escherichia coli ribosome at 23 Å resolution: fitting the ribosomal RNA. Structure 3: 815-821.
    • (1995) Structure , vol.3 , pp. 815-821
    • Stark, H.1    Mueller, F.2    Orlova, E.V.3    Schatz, M.4    Dube, P.5    Erdemir, T.6
  • 28
    • 0030887834 scopus 로고    scopus 로고
    • Arrangement of tRNAs in preand posttranslocational ribosomes revealed by electron cryomicroscopy
    • Stark, H., Orlova, E.V., Rinke-Apel, J., Jünke, N., Mueller, F., Rodnina, M.V., et al. (1997a) Arrangement of tRNAs in preand posttranslocational ribosomes revealed by electron cryomicroscopy. Cell 88: 19-28.
    • (1997) Cell , vol.88 , pp. 19-28
    • Stark, H.1    Orlova, E.V.2    Rinke-Apel, J.3    Jünke, N.4    Mueller, F.5    Rodnina, M.V.6
  • 30
    • 0031029466 scopus 로고    scopus 로고
    • Identification and purification of translation initiation factor 2 (IF2) from Thermus thermophilus
    • Vornlocher, H.-P., Scheible, W., Faulhammer, H., and Sprinzl, M. (1997) Identification and purification of translation initiation factor 2 (IF2) from Thermus thermophilus. Eur J Biochem 243: 66-71.
    • (1997) Eur J Biochem , vol.243 , pp. 66-71
    • Vornlocher, H.-P.1    Scheible, W.2    Faulhammer, H.3    Sprinzl, M.4
  • 31
    • 0024331948 scopus 로고
    • The solution structure of the Escherichia coli initiator tRNA and its interaction with initiation factor 2 and the ribosomal 3OS subunit
    • Wakao, H., Romby, P., Westhof, E., Laalami, S., Grunberg-Manago, M., Ebel, J.-P., et al. (1989) The solution structure of the Escherichia coli initiator tRNA and its interaction with initiation factor 2 and the ribosomal 3OS subunit. J Biol Chem 264: 20363-20371.
    • (1989) J Biol Chem , vol.264 , pp. 20363-20371
    • Wakao, H.1    Romby, P.2    Westhof, E.3    Laalami, S.4    Grunberg-Manago, M.5    Ebel, J.-P.6
  • 32
    • 0029835702 scopus 로고    scopus 로고
    • Ribosome-initiator tRNA complex as an intermediate in translation initiation in Escherichia coli revealed by use of mutant initiator tRNAs and specialized ribosomes
    • Wu, X.-Q., Iyengar, P., and RajBhandary, U.L. (1996) Ribosome-initiator tRNA complex as an intermediate in translation initiation in Escherichia coli revealed by use of mutant initiator tRNAs and specialized ribosomes. EMBO J 15: 4734-4739.
    • (1996) EMBO J , vol.15 , pp. 4734-4739
    • Wu, X.-Q.1    Iyengar, P.2    RajBhandary, U.L.3
  • 33
    • 0031026590 scopus 로고    scopus 로고
    • Effect of the aminoacid attached to Escherichia coli initiator tRNA on its affinity for the initiation factor IF2 and on the IF2 dependence of its binding to the ribosome
    • Wu, X.-Q., and RajBhandary, U.L. (1997) Effect of the aminoacid attached to Escherichia coli initiator tRNA on its affinity for the initiation factor IF2 and on the IF2 dependence of its binding to the ribosome. J Biol Chem 272: 1891-1895.
    • (1997) J Biol Chem , vol.272 , pp. 1891-1895
    • Wu, X.-Q.1    RajBhandary, U.L.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.