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Volumn 52, Issue 3-4, 2006, Pages 359-374

On ribosome conservation and evolution

Author keywords

Gene fusion; Peptide bond formation; Ribosomal symmetrical region; Ribosome evolution; Transition state

Indexed keywords

CATALYSIS; GENE EXPRESSION; PEPTIDE; POLYMERIZATION; RNA;

EID: 35548998339     PISSN: 15659801     EISSN: 22244662     Source Type: Journal    
DOI: 10.1560/IJEE_52_3-4_359     Document Type: Conference Paper
Times cited : (46)

References (46)
  • 3
    • 26844561217 scopus 로고    scopus 로고
    • Symmetry at the active site of the ribosome: Structural and functional implications
    • Agmon, I., Bashan, A., Zarivach, R., Yonath, A. 2005. Symmetry at the active site of the ribosome: structural and functional implications. Biol. Chem. 386: 833-844.
    • (2005) Biol. Chem , vol.386 , pp. 833-844
    • Agmon, I.1    Bashan, A.2    Zarivach, R.3    Yonath, A.4
  • 4
    • 0034637111 scopus 로고    scopus 로고
    • The complete atomic structure of the large ribosomal subunit at 2.4 A resolution
    • Ban, N., Nissen, P., Hansen, J., Moore, P.B., Steitz, T.A. 2000. The complete atomic structure of the large ribosomal subunit at 2.4 A resolution. Science 289: 905-920.
    • (2000) Science , vol.289 , pp. 905-920
    • Ban, N.1    Nissen, P.2    Hansen, J.3    Moore, P.B.4    Steitz, T.A.5
  • 5
    • 14544275165 scopus 로고    scopus 로고
    • From peptide-bond formation to cotranslational folding: Dynamic, regulatory and evolutionary aspects
    • Baram, D., Yonath, A. 2005. From peptide-bond formation to cotranslational folding: dynamic, regulatory and evolutionary aspects. FEBS Lett. 579: 948-954.
    • (2005) FEBS Lett , vol.579 , pp. 948-954
    • Baram, D.1    Yonath, A.2
  • 6
    • 24744435971 scopus 로고    scopus 로고
    • Structure of trigger factor binding domain in biologically homologous complex with eubacterial ribosome revealed its chaperone action
    • Baram, D., Pyetan, E., Sittner, A., Auerbach-Nevo, T., Bashan, A., Yonath, A. 2005. Structure of trigger factor binding domain in biologically homologous complex with eubacterial ribosome revealed its chaperone action. Proc. Natl. Acad. Sci. USA 102: 12017-12022.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 12017-12022
    • Baram, D.1    Pyetan, E.2    Sittner, A.3    Auerbach-Nevo, T.4    Bashan, A.5    Yonath, A.6
  • 9
    • 0035964256 scopus 로고    scopus 로고
    • A conformational change in the ribosomal peptidyl transferase center upon active/inactive transition
    • Bayfield, M.A., Dahlberg, A.E., Schulmeister, U., Dorner, S., Barta, A. 2001. A conformational change in the ribosomal peptidyl transferase center upon active/inactive transition. Proc. Natl. Acad. Sci. USA 98: 10096-10101.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 10096-10101
    • Bayfield, M.A.1    Dahlberg, A.E.2    Schulmeister, U.3    Dorner, S.4    Barta, A.5
  • 12
    • 0029402170 scopus 로고
    • Histidine 229 in protein L2 is apparently essential for 50S peptidyl transferase activity
    • Cooperman, B.S., Wooten, T., Romero, D.P., Traut, R.R. 1995. Histidine 229 in protein L2 is apparently essential for 50S peptidyl transferase activity. Biochem. Cell. Biol. 73: 1087-1094.
    • (1995) Biochem. Cell. Biol , vol.73 , pp. 1087-1094
    • Cooperman, B.S.1    Wooten, T.2    Romero, D.P.3    Traut, R.R.4
  • 13
    • 0034596998 scopus 로고    scopus 로고
    • Ribosomal protein L2 is involved in the association of the ribosomal subunits, tRNA binding to A- and P-sites and peptidyl transfer
    • Diedrich, G., Spahn, C.M., Stelzl, U., Schafer, M.A., Wooten, T., Bochkariov, D.E., Cooperman, B.S., Traut, R.R., Nierhaus, K.H. 2000. Ribosomal protein L2 is involved in the association of the ribosomal subunits, tRNA binding to A- and P-sites and peptidyl transfer. EMBO J. 19: 5241-5250.
    • (2000) EMBO J , vol.19 , pp. 5241-5250
    • Diedrich, G.1    Spahn, C.M.2    Stelzl, U.3    Schafer, M.A.4    Wooten, T.5    Bochkariov, D.E.6    Cooperman, B.S.7    Traut, R.R.8    Nierhaus, K.H.9
  • 16
    • 21844446585 scopus 로고    scopus 로고
    • Mutational analysis of 16S and 23S rRNA genes of Thermus thermophilus
    • Gregory, S.T., Carr, J.F., Rodriguez-Correa, D., Dahlberg, A.E. 2005. Mutational analysis of 16S and 23S rRNA genes of Thermus thermophilus. J. Bacteriol. 187: 4804-4812.
    • (2005) J. Bacteriol , vol.187 , pp. 4804-4812
    • Gregory, S.T.1    Carr, J.F.2    Rodriguez-Correa, D.3    Dahlberg, A.E.4
  • 19
    • 33644959635 scopus 로고    scopus 로고
    • Regiospecificity of the peptidyl tRNA ester within the ribosomal P-site
    • Huang, K.S., Weinger, J.S., Butler, E.B., Strobel, S.A. 2006. Regiospecificity of the peptidyl tRNA ester within the ribosomal P-site. J Am. Chem. Soc. 128: 3108-3109.
    • (2006) J Am. Chem. Soc , vol.128 , pp. 3108-3109
    • Huang, K.S.1    Weinger, J.S.2    Butler, E.B.3    Strobel, S.A.4
  • 21
    • 0033231562 scopus 로고    scopus 로고
    • Base-pairing between 23S rRNA and tRNA in the ribosomal A-site
    • Kim, D.F., Green, R. 1999. Base-pairing between 23S rRNA and tRNA in the ribosomal A-site. Mol. Cell 4: 859-864.
    • (1999) Mol. Cell , vol.4 , pp. 859-864
    • Kim, D.F.1    Green, R.2
  • 22
    • 0033090307 scopus 로고    scopus 로고
    • Dimer formation by tRNAs
    • Kholod, N.S. 1999. Dimer formation by tRNAs. Biochemistry (Moscow) 64: 298-306.
    • (1999) Biochemistry (Moscow) , vol.64 , pp. 298-306
    • Kholod, N.S.1
  • 23
    • 33748582906 scopus 로고    scopus 로고
    • Crystal structure of a 70S ribosome-tRNA complex reveals functional interactions and rearrangements
    • Korostelev, A., Trakhanov, S., Laurberg, M., Noller, 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    Noller, H.F.4
  • 24
    • 0030806152 scopus 로고    scopus 로고
    • A conformational switch in Escherichia coli 16S RNA during decoding of messenger RNA
    • Lodmell, J.S., Dahlberg, A.E. 1997. A conformational switch in Escherichia coli 16S RNA during decoding of messenger RNA. Science 277: 1262-1267.
    • (1997) Science , vol.277 , pp. 1262-1267
    • Lodmell, J.S.1    Dahlberg, A.E.2
  • 25
    • 27644598282 scopus 로고    scopus 로고
    • A protein component at the heart of an RNA machine: The importance of protein 127 for the function of the bacterial ribosome
    • Maguire, B.A., Beniaminov, A.D., Ramu, H., Mankin, A.S., Zimmermann, R.A. 2005. A protein component at the heart of an RNA machine: the importance of protein 127 for the function of the bacterial ribosome. Mol. Cell 20: 427-435.
    • (2005) Mol. Cell , vol.20 , pp. 427-435
    • Maguire, B.A.1    Beniaminov, A.D.2    Ramu, H.3    Mankin, A.S.4    Zimmermann, R.A.5
  • 27
    • 37049243502 scopus 로고
    • A production of amino acids under possible primitive earth conditions
    • Miller S.L. 1953. A production of amino acids under possible primitive earth conditions. Science 117:529-529.
    • (1953) Science , vol.117 , pp. 529-529
    • Miller, S.L.1
  • 28
    • 0034637161 scopus 로고    scopus 로고
    • The structural basis of ribosome activity in peptide bond synthesis
    • Nissen, P., Hansen, J., Ban, N., Moore, RB., Steitz, T.A. 2000. The structural basis of ribosome activity in peptide bond synthesis. Science 289: 920-930.
    • (2000) Science , vol.289 , pp. 920-930
    • Nissen, P.1    Hansen, J.2    Ban, N.3    Moore, R.B.4    Steitz, T.A.5
  • 29
    • 0026315514 scopus 로고
    • Folding of circularly permuted transfer RNAs
    • Pan, T., Gutell, R.R., Uhlenbeck, O.C. 1991. Folding of circularly permuted transfer RNAs. Science 254: 1361-1364.
    • (1991) Science , vol.254 , pp. 1361-1364
    • Pan, T.1    Gutell, R.R.2    Uhlenbeck, O.C.3
  • 31
    • 13944256506 scopus 로고    scopus 로고
    • Structural probing of a pathogenic tRNA dimer
    • Roy, M.D., Wittenhagen, L.M., Kelley, S.O. 2005. Structural probing of a pathogenic tRNA dimer, RNA 11: 254-260.
    • (2005) RNA , vol.11 , pp. 254-260
    • Roy, M.D.1    Wittenhagen, L.M.2    Kelley, S.O.3
  • 32
    • 33750359363 scopus 로고    scopus 로고
    • Comprehensive genetic selection revealed bases essential for protein synthesis in the peptidyl-transferase center
    • Sato, N.Z., Hirabayashi, N., Agmon, I., Yonath, A., Suzuki, T. 2006, Comprehensive genetic selection revealed bases essential for protein synthesis in the peptidyl-transferase center. Proc. Natl. Acad. Sci. USA 193:15386-15391.
    • (2006) Proc. Natl. Acad. Sci. USA , vol.193 , pp. 15386-15391
    • Sato, N.Z.1    Hirabayashi, N.2    Agmon, I.3    Yonath, A.4    Suzuki, T.5
  • 35
    • 27644557445 scopus 로고    scopus 로고
    • Structural insights into the roles of water and the 2′ hydroxyl of the P-site tRNA in the peptidyl transferase reaction
    • Schmeing, T.M., Huang, K.S., Kitchen, D.E., Strobel, S.A., Steitz, T.A. 2005a. Structural insights into the roles of water and the 2′ hydroxyl of the P-site tRNA in the peptidyl transferase reaction. Mol. Cell 20: 437-448.
    • (2005) Mol. Cell , vol.20 , pp. 437-448
    • Schmeing, T.M.1    Huang, K.S.2    Kitchen, D.E.3    Strobel, S.A.4    Steitz, T.A.5
  • 36
    • 28544452248 scopus 로고    scopus 로고
    • An induced-fit mechanism to promote peptide bond formation and exclude hydrolysis of peptidyl-tRNA
    • Schmeing, T.M., Huang, K.S., Strobel, S.A., Steitz, T.A. 2005b. An induced-fit mechanism to promote peptide bond formation and exclude hydrolysis of peptidyl-tRNA. Nature 438: 520-524.
    • (2005) Nature , vol.438 , pp. 520-524
    • Schmeing, T.M.1    Huang, K.S.2    Strobel, S.A.3    Steitz, T.A.4
  • 39
    • 27744581953 scopus 로고    scopus 로고
    • Conserved sequences of prokaryotic proteomes and their compositional age
    • Sobolevsky, Y., Trifonov, E.N. 2005. Conserved sequences of prokaryotic proteomes and their compositional age. J. Mol. Evol. 61: 591-596.
    • (2005) J. Mol. Evol , vol.61 , pp. 591-596
    • Sobolevsky, Y.1    Trifonov, E.N.2
  • 40
    • 10244226778 scopus 로고    scopus 로고
    • Testing the conservation of the translational machinery over evolution in diverse environments: Assaying Thermus thermophilus ribosomes and initiation factors in a coupled transcription-translation system from Escherichia coli
    • Thompson, J., Dahlberg, A.E. 2004. Testing the conservation of the translational machinery over evolution in diverse environments: assaying Thermus thermophilus ribosomes and initiation factors in a coupled transcription-translation system from Escherichia coli. Nucleic Acids Res. 32:5954-5961.
    • (2004) Nucleic Acids Res , vol.32 , pp. 5954-5961
    • Thompson, J.1    Dahlberg, A.E.2
  • 43
    • 0344253692 scopus 로고    scopus 로고
    • Ribosomal tolerance and peptide bond formation
    • Yonath, A. 2003. Ribosomal tolerance and peptide bond formation. Biol. Chem. 384: 1411-1419.
    • (2003) Biol. Chem , vol.384 , pp. 1411-1419
    • Yonath, A.1
  • 45
    • 0015223366 scopus 로고
    • Inactivation and reactivation of ribosomal subunits: Amino acyl transfer RNA binding activity of the 30S subunit from E. coli
    • Zamir, A., Miskin, R., Elson, D. 1971. Inactivation and reactivation of ribosomal subunits: amino acyl transfer RNA binding activity of the 30S subunit from E. 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.