Essential Mechanisms in the Catalysis of Peptide Bond Formation on the Ribosome
Peptide bond formation is the main catalytic function of the ribo-some. The mechanism of catalysis is presumed to be highly conserved in all organisms. We tested the conservation by comparing mechanistic features of the peptidyl transfer reaction on ribosomes from Escherichia coli and the Gram-posit...
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Published in | The Journal of biological chemistry Vol. 280; no. 43; pp. 36065 - 36072 |
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Main Authors | , , , , , , , , |
Format | Journal Article |
Language | English |
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United States
Elsevier Inc
28.10.2005
American Society for Biochemistry and Molecular Biology |
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Abstract | Peptide bond formation is the main catalytic function of the ribo-some. The mechanism of catalysis is presumed to be highly conserved in all organisms. We tested the conservation by comparing mechanistic features of the peptidyl transfer reaction on ribosomes from Escherichia coli and the Gram-positive bacterium Mycobacterium smegmatis. In both cases, the major contribution to catalysis was the lowering of the activation entropy. The rate of peptide bond formation was pH independent with the natural substrate, amino-acyl-tRNA, but was slowed down 200-fold with decreasing pH when puromycin was used as a substrate analog. Mutation of the conserved base A2451 of 23 S rRNA to U did not abolish the pH dependence of the reaction with puromycin in M. smegmatis, suggesting that A2451 did not confer the pH dependence. However, the A2451U mutation alters the structure of the peptidyl transferase center and changes the pattern of pH-dependent rearrangements, as probed by chemical modification of 23 S rRNA. A2451 seems to function as a pivot point in ordering the structure of the peptidyl transferase center rather than taking part in chemical catalysis. |
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AbstractList | Peptide bond formation is the main catalytic function of the ribosome. The mechanism of catalysis is presumed to be highly conserved in all organisms. We tested the conservation by comparing mechanistic features of the peptidyl transfer reaction on ribosomes from Escherichia coli and the Gram-positive bacterium Mycobacterium smegmatis. In both cases, the major contribution to catalysis was the lowering of the activation entropy. The rate of peptide bond formation was pH independent with the natural substrate, amino-acyl-tRNA, but was slowed down 200-fold with decreasing pH when puromycin was used as a substrate analog. Mutation of the conserved base A2451 of 23 S rRNA to U did not abolish the pH dependence of the reaction with puromycin in M. smegmatis, suggesting that A2451 did not confer the pH dependence. However, the A2451U mutation alters the structure of the peptidyl transferase center and changes the pattern of pH-dependent rearrangements, as probed by chemical modification of 23 S rRNA. A2451 seems to function as a pivot point in ordering the structure of the peptidyl transferase center rather than taking part in chemical catalysis. Peptide bond formation is the main catalytic function of the ribo-some. The mechanism of catalysis is presumed to be highly conserved in all organisms. We tested the conservation by comparing mechanistic features of the peptidyl transfer reaction on ribosomes from Escherichia coli and the Gram-positive bacterium Mycobacterium smegmatis . In both cases, the major contribution to catalysis was the lowering of the activation entropy. The rate of peptide bond formation was pH independent with the natural substrate, amino-acyl-tRNA, but was slowed down 200-fold with decreasing pH when puromycin was used as a substrate analog. Mutation of the conserved base A2451 of 23 S rRNA to U did not abolish the pH dependence of the reaction with puromycin in M. smegmatis , suggesting that A2451 did not confer the pH dependence. However, the A2451U mutation alters the structure of the peptidyl transferase center and changes the pattern of pH-dependent rearrangements, as probed by chemical modification of 23 S rRNA. A2451 seems to function as a pivot point in ordering the structure of the peptidyl transferase center rather than taking part in chemical catalysis. Peptide bond formation is the main catalytic function of the ribo-some. The mechanism of catalysis is presumed to be highly conserved in all organisms. We tested the conservation by comparing mechanistic features of the peptidyl transfer reaction on ribosomes from Escherichia coli and the Gram-positive bacterium Mycobacterium smegmatis. In both cases, the major contribution to catalysis was the lowering of the activation entropy. The rate of peptide bond formation was pH independent with the natural substrate, amino-acyl-tRNA, but was slowed down 200-fold with decreasing pH when puromycin was used as a substrate analog. Mutation of the conserved base A2451 of 23 S rRNA to U did not abolish the pH dependence of the reaction with puromycin in M. smegmatis, suggesting that A2451 did not confer the pH dependence. However, the A2451U mutation alters the structure of the peptidyl transferase center and changes the pattern of pH-dependent rearrangements, as probed by chemical modification of 23 S rRNA. A2451 seems to function as a pivot point in ordering the structure of the peptidyl transferase center rather than taking part in chemical catalysis. |
Author | Beringer, Malte Bieling, Peter Xiong, Liqun Pfister, Peter Böttger, Erik C. Katunin, Vladimir I. Bruell, Christian Rodnina, Marina V. Mankin, Alexander S. |
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BackLink | https://www.ncbi.nlm.nih.gov/pubmed/16129670$$D View this record in MEDLINE/PubMed |
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Cites_doi | 10.1038/nsmb841 10.1016/S0092-8674(01)00546-3 10.1093/nar/gkh888 10.1073/pnas.92.6.1945 10.1038/35078113 10.1016/S1097-2765(02)00566-X 10.1016/S0092-8674(04)00411-8 10.1073/pnas.171319598 10.1073/pnas.172404099 10.1016/j.jmb.2004.11.073 10.1016/S1097-2765(03)00009-1 10.1111/j.1432-1033.1968.tb00450.x 10.1126/science.289.5481.905 10.1146/annurev.biochem.72.110601.135450 10.1073/pnas.182210099 10.1261/rna.5600503 10.1073/pnas.0402488101 10.1046/j.1365-2958.1996.01532.x 10.1016/0006-291X(68)90330-6 10.1093/emboj/17.24.7490 10.1093/nar/gki308 10.1126/science.6163215 10.1021/bi00905a031 10.1016/S0079-6603(08)60809-0 10.1016/S0079-6603(08)60348-7 10.1038/290607a0 10.1002/cbic.200300657 10.1073/pnas.96.17.9586 10.1128/AAC.43.3.447 10.1126/science.289.5481.947 10.1046/j.1365-2958.2002.03242.x 10.1126/science.289.5481.920 10.1093/nar/gkh672 10.1073/pnas.151257098 10.1002/bip.10519 |
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References | Polacek, Gaynor, Yassin, Mankin (bib16) 2001; 411 Bashan, Agmon, Zarivach, Schluenzen, Harms, Berisio, Bartels, Franceschi, Auerbach, Hansen, Kossoy, Kessler, Yonath (bib35) 2003; 11 Muth, Chen, Kosek, Strobel (bib38) 2001; 7 Bayfield, Dahlberg, Schulmeister, Dorner, Barta (bib30) 2001; 98 Miskin, Zamir, Elson (bib37) 1968; 33 Bayfield, Thompson, Dahlberg (bib40) 2004; 32 Weinger, Parnell, Dorner, Green, Strobel (bib21) 2004; 11 Thompson, Kim, O'Connor, Lieberman, Bayfield, Gregory, Green, Noller, Dahlberg (bib14) 2001; 98 Kearsey, Craig (bib41) 1981; 290 Wolfenden (bib3) 1963; 338 Gutell, Weiser, Woese, Noller (bib32) 1985; 32 Moore, Steitz (bib8) 2003; 72 Pfister, Hobbie, Brull, Corti, Vasella, Westhof, Bottger (bib22) 2005; 346 Pape, Wintermeyer, Rodnina (bib36) 1998; 17 Rodnina, Savelsbergh, Matassova, Katunin, Semenkov, Wintermeyer (bib28) 1999; 96 Beringer, Adio, Wintermeyer, Rodnina (bib19) 2003; 9 Pfister, Hobbie, Vicens, Bottger, Westhof (bib23) 2003; 4 Merryman, Noller (bib29) 1998 Sievers, Beringer, Rodnina, Wolfenden (bib17) 2004; 101 Muth, Ortoleva-Donnelly, Strobel (bib15) 2000; 289 Sander, Belova, Kidan, Pfister, Mankin, Bottger (bib24) 2002; 46 Nierhaus, Schulze, Cooperman (bib9) 1980; 1 Erlacher, Lang, Shankaran, Wotzel, Huttenhofer, Micura, Mankin, Polacek (bib12) 2005; 33 Hesslein, Katunin, Beringer, Kosek, Rodnina, Strobel (bib31) 2004; 32 Noller, Woese (bib33) 1981; 212 Maden, Monro (bib7) 1968; 6 Prammananan, Sander, Springer, Bottger (bib26) 1999; 43 Xiong, Polacek, Sander, Bottger, Mankin (bib39) 2001; 7 Krayevsky, Kukhanova (bib5) 1979; 23 Harms, Schluenzen, Zarivach, Bashan, Gat, Agmon, Bartels, Franceschi, Yonath (bib34) 2001; 107 Nissen, Hansen, Ban, Moore, Steitz (bib2) 2000; 289 Barta, Halama (bib4) 1996 Sander, Prammananan, Bottger (bib25) 1996; 22 Rodnina, Wintermeyer (bib27) 1995; 92 Lieberman, Dahlberg (bib6) 1995; 50 Parnell, Seila, Strobel (bib13) 2002; 99 Katunin, Muth, Strobel, Wintermeyer, Rodnina (bib10) 2002; 10 Hansen, Schmeing, Moore, Steitz (bib11) 2002; 99 Youngman, Brunelle, Kochaniak, Green (bib18) 2004; 117 Bevilacqua, Brown, Nakano, Yajima (bib20) 2004; 73 Ban, Nissen, Hansen, Moore, Steitz (bib1) 2000; 289 Parnell (10.1074/jbc.M507961200_bib13) 2002; 99 Krayevsky (10.1074/jbc.M507961200_bib5) 1979; 23 Sander (10.1074/jbc.M507961200_bib25) 1996; 22 Gutell (10.1074/jbc.M507961200_bib32) 1985; 32 Bashan (10.1074/jbc.M507961200_bib35) 2003; 11 Beringer (10.1074/jbc.M507961200_bib19) 2003; 9 Bayfield (10.1074/jbc.M507961200_bib40) 2004; 32 Pfister (10.1074/jbc.M507961200_bib23) 2003; 4 Polacek (10.1074/jbc.M507961200_bib16) 2001; 411 Bayfield (10.1074/jbc.M507961200_bib30) 2001; 98 Hansen (10.1074/jbc.M507961200_bib11) 2002; 99 Sander (10.1074/jbc.M507961200_bib24) 2002; 46 Erlacher (10.1074/jbc.M507961200_bib12) 2005; 33 Pfister (10.1074/jbc.M507961200_bib22) 2005; 346 Wolfenden (10.1074/jbc.M507961200_bib3) 1963; 338 Rodnina (10.1074/jbc.M507961200_bib28) 1999; 96 Pape (10.1074/jbc.M507961200_bib36) 1998; 17 Katunin (10.1074/jbc.M507961200_bib10) 2002; 10 Prammananan (10.1074/jbc.M507961200_bib26) 1999; 43 Muth (10.1074/jbc.M507961200_bib15) 2000; 289 Bevilacqua (10.1074/jbc.M507961200_bib20) 2004; 73 Miskin (10.1074/jbc.M507961200_bib37) 1968; 33 Lieberman (10.1074/jbc.M507961200_bib6) 1995; 50 Moore (10.1074/jbc.M507961200_bib8) 2003; 72 Xiong (10.1074/jbc.M507961200_bib39) 2001; 7 Harms (10.1074/jbc.M507961200_bib34) 2001; 107 Merryman (10.1074/jbc.M507961200_bib29) 1998 Hesslein (10.1074/jbc.M507961200_bib31) 2004; 32 Maden (10.1074/jbc.M507961200_bib7) 1968; 6 Sievers (10.1074/jbc.M507961200_bib17) 2004; 101 Kearsey (10.1074/jbc.M507961200_bib41) 1981; 290 Muth (10.1074/jbc.M507961200_bib38) 2001; 7 Thompson (10.1074/jbc.M507961200_bib14) 2001; 98 Noller (10.1074/jbc.M507961200_bib33) 1981; 212 Nissen (10.1074/jbc.M507961200_bib2) 2000; 289 Ban (10.1074/jbc.M507961200_bib1) 2000; 289 Weinger (10.1074/jbc.M507961200_bib21) 2004; 11 Barta (10.1074/jbc.M507961200_bib4) 1996 Nierhaus (10.1074/jbc.M507961200_bib9) 1980; 1 Youngman (10.1074/jbc.M507961200_bib18) 2004; 117 Rodnina (10.1074/jbc.M507961200_bib27) 1995; 92 |
References_xml | – volume: 1 start-page: 185 year: 1980 end-page: 192 ident: bib9 publication-title: Biochem. Int. contributor: fullname: Cooperman – volume: 92 start-page: 1945 year: 1995 end-page: 1949 ident: bib27 publication-title: Proc. Natl. Acad. Sci. U. S. A. contributor: fullname: Wintermeyer – volume: 33 start-page: 1618 year: 2005 end-page: 1627 ident: bib12 publication-title: Nucleic Acids Res. contributor: fullname: Polacek – volume: 117 start-page: 589 year: 2004 end-page: 599 ident: bib18 publication-title: Cell contributor: fullname: Green – volume: 338 start-page: 1090 year: 1963 end-page: 1092 ident: bib3 publication-title: Biochemistry contributor: fullname: Wolfenden – volume: 289 start-page: 920 year: 2000 end-page: 930 ident: bib2 publication-title: Science contributor: fullname: Steitz – volume: 73 start-page: 90 year: 2004 end-page: 109 ident: bib20 publication-title: Biopolymers contributor: fullname: Yajima – volume: 289 start-page: 947 year: 2000 end-page: 950 ident: bib15 publication-title: Science contributor: fullname: Strobel – volume: 107 start-page: 679 year: 2001 end-page: 688 ident: bib34 publication-title: Cell contributor: fullname: Yonath – volume: 43 start-page: 447 year: 1999 end-page: 453 ident: bib26 publication-title: Antimicrob. Agents Chemother. contributor: fullname: Bottger – volume: 11 start-page: 1101 year: 2004 end-page: 1106 ident: bib21 publication-title: Nat. Struct. Mol. Biol. contributor: fullname: Strobel – volume: 101 start-page: 7897 year: 2004 end-page: 7901 ident: bib17 publication-title: Proc. Natl. Acad. Sci. U. S. A. contributor: fullname: Wolfenden – volume: 7 start-page: 1403 year: 2001 end-page: 1415 ident: bib38 publication-title: RNA (N.Y.) contributor: fullname: Strobel – volume: 99 start-page: 11658 year: 2002 end-page: 11663 ident: bib13 publication-title: Proc. Natl. Acad. Sci. U. S. A. contributor: fullname: Strobel – volume: 72 start-page: 813 year: 2003 end-page: 850 ident: bib8 publication-title: Annu. Rev. Biochem. contributor: fullname: Steitz – volume: 10 start-page: 339 year: 2002 end-page: 346 ident: bib10 publication-title: Mol. Cell contributor: fullname: Rodnina – volume: 22 start-page: 841 year: 1996 end-page: 848 ident: bib25 publication-title: Mol. Microbiol. contributor: fullname: Bottger – volume: 32 start-page: 155 year: 1985 end-page: 216 ident: bib32 publication-title: Prog. Nucleic Acids Res. Mol. Biol. contributor: fullname: Noller – volume: 7 start-page: 1365 year: 2001 end-page: 1369 ident: bib39 publication-title: RNA (N.Y.) contributor: fullname: Mankin – volume: 99 start-page: 11670 year: 2002 end-page: 11675 ident: bib11 publication-title: Proc. Natl. Acad. Sci. U. S. A. contributor: fullname: Steitz – volume: 32 start-page: 3760 year: 2004 end-page: 3770 ident: bib31 publication-title: Nucleic Acids Res. contributor: fullname: Strobel – volume: 4 start-page: 1078 year: 2003 end-page: 1088 ident: bib23 publication-title: Chembiochem. contributor: fullname: Westhof – volume: 96 start-page: 9586 year: 1999 end-page: 9590 ident: bib28 publication-title: Proc. Natl. Acad. Sci. U. S. A. contributor: fullname: Wintermeyer – volume: 23 start-page: 1 year: 1979 end-page: 51 ident: bib5 publication-title: Prog. Nucleic Acids Res. Mol. Biol. contributor: fullname: Kukhanova – volume: 346 start-page: 467 year: 2005 end-page: 475 ident: bib22 publication-title: J. Mol. Biol. contributor: fullname: Bottger – volume: 50 start-page: 1 year: 1995 end-page: 23 ident: bib6 publication-title: Prog. Nucleic Acids Res. Mol. Biol. contributor: fullname: Dahlberg – start-page: 35 year: 1996 end-page: 54 ident: bib4 publication-title: Ribosomal RNA and Group I Introns contributor: fullname: Halama – volume: 289 start-page: 905 year: 2000 end-page: 920 ident: bib1 publication-title: Science contributor: fullname: Steitz – volume: 6 start-page: 309 year: 1968 end-page: 316 ident: bib7 publication-title: Eur. J. Biochem. contributor: fullname: Monro – volume: 290 start-page: 607 year: 1981 end-page: 608 ident: bib41 publication-title: Nature contributor: fullname: Craig – volume: 32 start-page: 5512 year: 2004 end-page: 5518 ident: bib40 publication-title: Nucleic Acids Res. contributor: fullname: Dahlberg – volume: 411 start-page: 498 year: 2001 end-page: 501 ident: bib16 publication-title: Nature contributor: fullname: Mankin – volume: 212 start-page: 403 year: 1981 end-page: 411 ident: bib33 publication-title: Science contributor: fullname: Woese – volume: 33 start-page: 551 year: 1968 end-page: 557 ident: bib37 publication-title: Biochem. Biophys. Res. Commun. contributor: fullname: Elson – volume: 98 start-page: 9002 year: 2001 end-page: 9007 ident: bib14 publication-title: Proc. Natl. Acad. Sci. U. S. A. contributor: fullname: Dahlberg – volume: 11 start-page: 91 year: 2003 end-page: 102 ident: bib35 publication-title: Mol. Cell contributor: fullname: Yonath – start-page: 237 year: 1998 end-page: 253 ident: bib29 publication-title: RNA:Protein Interactions, A Practical Approach contributor: fullname: Noller – volume: 46 start-page: 1295 year: 2002 end-page: 1304 ident: bib24 publication-title: Mol. Microbiol. contributor: fullname: Bottger – volume: 17 start-page: 7490 year: 1998 end-page: 7497 ident: bib36 publication-title: EMBO J. contributor: fullname: Rodnina – volume: 9 start-page: 919 year: 2003 end-page: 922 ident: bib19 publication-title: RNA (N.Y.) contributor: fullname: Rodnina – volume: 98 start-page: 10096 year: 2001 end-page: 10101 ident: bib30 publication-title: Proc. Natl. Acad. Sci. U. S. A. contributor: fullname: Barta – volume: 11 start-page: 1101 year: 2004 ident: 10.1074/jbc.M507961200_bib21 publication-title: Nat. Struct. Mol. Biol. doi: 10.1038/nsmb841 contributor: fullname: Weinger – volume: 107 start-page: 679 year: 2001 ident: 10.1074/jbc.M507961200_bib34 publication-title: Cell doi: 10.1016/S0092-8674(01)00546-3 contributor: fullname: Harms – volume: 32 start-page: 5512 year: 2004 ident: 10.1074/jbc.M507961200_bib40 publication-title: Nucleic Acids Res. doi: 10.1093/nar/gkh888 contributor: fullname: Bayfield – volume: 92 start-page: 1945 year: 1995 ident: 10.1074/jbc.M507961200_bib27 publication-title: Proc. Natl. Acad. Sci. U. S. A. doi: 10.1073/pnas.92.6.1945 contributor: fullname: Rodnina – volume: 411 start-page: 498 year: 2001 ident: 10.1074/jbc.M507961200_bib16 publication-title: Nature doi: 10.1038/35078113 contributor: fullname: Polacek – start-page: 35 year: 1996 ident: 10.1074/jbc.M507961200_bib4 contributor: fullname: Barta – volume: 10 start-page: 339 year: 2002 ident: 10.1074/jbc.M507961200_bib10 publication-title: Mol. Cell doi: 10.1016/S1097-2765(02)00566-X contributor: fullname: Katunin – volume: 117 start-page: 589 year: 2004 ident: 10.1074/jbc.M507961200_bib18 publication-title: Cell doi: 10.1016/S0092-8674(04)00411-8 contributor: fullname: Youngman – volume: 7 start-page: 1365 year: 2001 ident: 10.1074/jbc.M507961200_bib39 publication-title: RNA (N.Y.) contributor: fullname: Xiong – volume: 98 start-page: 10096 year: 2001 ident: 10.1074/jbc.M507961200_bib30 publication-title: Proc. Natl. Acad. Sci. U. S. A. doi: 10.1073/pnas.171319598 contributor: fullname: Bayfield – volume: 99 start-page: 11670 year: 2002 ident: 10.1074/jbc.M507961200_bib11 publication-title: Proc. Natl. Acad. Sci. U. S. A. doi: 10.1073/pnas.172404099 contributor: fullname: Hansen – volume: 346 start-page: 467 year: 2005 ident: 10.1074/jbc.M507961200_bib22 publication-title: J. Mol. Biol. doi: 10.1016/j.jmb.2004.11.073 contributor: fullname: Pfister – volume: 11 start-page: 91 year: 2003 ident: 10.1074/jbc.M507961200_bib35 publication-title: Mol. Cell doi: 10.1016/S1097-2765(03)00009-1 contributor: fullname: Bashan – volume: 6 start-page: 309 year: 1968 ident: 10.1074/jbc.M507961200_bib7 publication-title: Eur. J. Biochem. doi: 10.1111/j.1432-1033.1968.tb00450.x contributor: fullname: Maden – volume: 7 start-page: 1403 year: 2001 ident: 10.1074/jbc.M507961200_bib38 publication-title: RNA (N.Y.) contributor: fullname: Muth – volume: 289 start-page: 905 year: 2000 ident: 10.1074/jbc.M507961200_bib1 publication-title: Science doi: 10.1126/science.289.5481.905 contributor: fullname: Ban – volume: 72 start-page: 813 year: 2003 ident: 10.1074/jbc.M507961200_bib8 publication-title: Annu. Rev. Biochem. doi: 10.1146/annurev.biochem.72.110601.135450 contributor: fullname: Moore – volume: 99 start-page: 11658 year: 2002 ident: 10.1074/jbc.M507961200_bib13 publication-title: Proc. Natl. Acad. Sci. U. S. A. doi: 10.1073/pnas.182210099 contributor: fullname: Parnell – volume: 9 start-page: 919 year: 2003 ident: 10.1074/jbc.M507961200_bib19 publication-title: RNA (N.Y.) doi: 10.1261/rna.5600503 contributor: fullname: Beringer – volume: 101 start-page: 7897 year: 2004 ident: 10.1074/jbc.M507961200_bib17 publication-title: Proc. Natl. Acad. Sci. U. S. A. doi: 10.1073/pnas.0402488101 contributor: fullname: Sievers – volume: 22 start-page: 841 year: 1996 ident: 10.1074/jbc.M507961200_bib25 publication-title: Mol. Microbiol. doi: 10.1046/j.1365-2958.1996.01532.x contributor: fullname: Sander – volume: 33 start-page: 551 year: 1968 ident: 10.1074/jbc.M507961200_bib37 publication-title: Biochem. Biophys. Res. Commun. doi: 10.1016/0006-291X(68)90330-6 contributor: fullname: Miskin – volume: 1 start-page: 185 year: 1980 ident: 10.1074/jbc.M507961200_bib9 publication-title: Biochem. Int. contributor: fullname: Nierhaus – volume: 17 start-page: 7490 year: 1998 ident: 10.1074/jbc.M507961200_bib36 publication-title: EMBO J. doi: 10.1093/emboj/17.24.7490 contributor: fullname: Pape – volume: 33 start-page: 1618 year: 2005 ident: 10.1074/jbc.M507961200_bib12 publication-title: Nucleic Acids Res. doi: 10.1093/nar/gki308 contributor: fullname: Erlacher – volume: 212 start-page: 403 year: 1981 ident: 10.1074/jbc.M507961200_bib33 publication-title: Science doi: 10.1126/science.6163215 contributor: fullname: Noller – start-page: 237 year: 1998 ident: 10.1074/jbc.M507961200_bib29 contributor: fullname: Merryman – volume: 338 start-page: 1090 year: 1963 ident: 10.1074/jbc.M507961200_bib3 publication-title: Biochemistry doi: 10.1021/bi00905a031 contributor: fullname: Wolfenden – volume: 50 start-page: 1 year: 1995 ident: 10.1074/jbc.M507961200_bib6 publication-title: Prog. Nucleic Acids Res. Mol. Biol. doi: 10.1016/S0079-6603(08)60809-0 contributor: fullname: Lieberman – volume: 32 start-page: 155 year: 1985 ident: 10.1074/jbc.M507961200_bib32 publication-title: Prog. Nucleic Acids Res. Mol. Biol. doi: 10.1016/S0079-6603(08)60348-7 contributor: fullname: Gutell – volume: 290 start-page: 607 year: 1981 ident: 10.1074/jbc.M507961200_bib41 publication-title: Nature doi: 10.1038/290607a0 contributor: fullname: Kearsey – volume: 4 start-page: 1078 year: 2003 ident: 10.1074/jbc.M507961200_bib23 publication-title: Chembiochem. doi: 10.1002/cbic.200300657 contributor: fullname: Pfister – volume: 96 start-page: 9586 year: 1999 ident: 10.1074/jbc.M507961200_bib28 publication-title: Proc. Natl. Acad. Sci. U. S. A. doi: 10.1073/pnas.96.17.9586 contributor: fullname: Rodnina – volume: 43 start-page: 447 year: 1999 ident: 10.1074/jbc.M507961200_bib26 publication-title: Antimicrob. Agents Chemother. doi: 10.1128/AAC.43.3.447 contributor: fullname: Prammananan – volume: 289 start-page: 947 year: 2000 ident: 10.1074/jbc.M507961200_bib15 publication-title: Science doi: 10.1126/science.289.5481.947 contributor: fullname: Muth – volume: 46 start-page: 1295 year: 2002 ident: 10.1074/jbc.M507961200_bib24 publication-title: Mol. Microbiol. doi: 10.1046/j.1365-2958.2002.03242.x contributor: fullname: Sander – volume: 289 start-page: 920 year: 2000 ident: 10.1074/jbc.M507961200_bib2 publication-title: Science doi: 10.1126/science.289.5481.920 contributor: fullname: Nissen – volume: 32 start-page: 3760 year: 2004 ident: 10.1074/jbc.M507961200_bib31 publication-title: Nucleic Acids Res. doi: 10.1093/nar/gkh672 contributor: fullname: Hesslein – volume: 23 start-page: 1 year: 1979 ident: 10.1074/jbc.M507961200_bib5 publication-title: Prog. Nucleic Acids Res. Mol. Biol. contributor: fullname: Krayevsky – volume: 98 start-page: 9002 year: 2001 ident: 10.1074/jbc.M507961200_bib14 publication-title: Proc. Natl. Acad. Sci. U. S. A. doi: 10.1073/pnas.151257098 contributor: fullname: Thompson – volume: 73 start-page: 90 year: 2004 ident: 10.1074/jbc.M507961200_bib20 publication-title: Biopolymers doi: 10.1002/bip.10519 contributor: fullname: Bevilacqua |
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Snippet | Peptide bond formation is the main catalytic function of the ribo-some. The mechanism of catalysis is presumed to be highly conserved in all organisms. We... Peptide bond formation is the main catalytic function of the ribo-some. The mechanism of catalysis is presumed to be highly conserved in all organisms. We... Peptide bond formation is the main catalytic function of the ribosome. The mechanism of catalysis is presumed to be highly conserved in all organisms. We... |
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SubjectTerms | Alleles Binding Sites Catalysis Conserved Sequence Entropy Escherichia coli Escherichia coli - metabolism Hydrogen-Ion Concentration Kinetics Mutagenesis Mutation Mycobacterium smegmatis Mycobacterium smegmatis - metabolism Peptides - chemistry Plasmids - metabolism Point Mutation Protein Conformation Puromycin - chemistry Puromycin - pharmacology Ribosomes - chemistry Ribosomes - metabolism RNA - chemistry RNA, Ribosomal, 23S - chemistry RNA, Transfer - chemistry Substrate Specificity Thermodynamics Time Factors |
Title | Essential Mechanisms in the Catalysis of Peptide Bond Formation on the Ribosome |
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