Abstract
▪ Abstract The underlying basis for the accuracy of protein synthesis has been the subject of over four decades of investigation. Recent biochemical and structural data make it possible to understand at least in outline the structural basis for tRNA selection, in which codon recognition by cognate tRNA results in the hydrolysis of GTP by EF-Tu over 75 Å away. The ribosome recognizes the geometry of codon-anticodon base pairing at the first two positions but monitors the third, or wobble position, less stringently. Part of the additional binding energy of cognate tRNA is used to induce conformational changes in the ribosome that stabilize a transition state for GTP hydrolysis by EF-Tu and subsequently result in accelerated accommodation of tRNA into the peptidyl transferase center. The transition state for GTP hydrolysis is characterized, among other things, by a distorted tRNA. This picture explains a large body of data on the effect of antibiotics and mutations on translational fidelity. However, many fundamental questions remain, such as the mechanism of activation of GTP hydrolysis by EF-Tu, and the relationship between decoding and frameshifting.
References
210
Referenced
507
10.1146/annurev.biochem.69.1.497
10.1007/BF00268784
10.1007/BF00334815
- Kurland CG, Hughes D, Ehrenberg M. 1996. InEscherichia coli and Salmonella typhimurium: Cellular and Molecular Biology, ed.FC Neidhardt, R Curtiss III, JL Ingraham, ECC Lin, KB Low, B Magasanik, pp.979–1004. Washington, DC: Am. Soc. Microbiol. Press
{'key': 'B5', 'volume-title': 'Structure and Mechanism in Protein Science', 'author': 'Fersht AR', 'year': '1998'}
/ Structure and Mechanism in Protein Science by Fersht AR (1998)10.1021/bi00624a034
10.1126/science.280.5363.578
10.1016/S0092-8674(00)00191-4
10.1021/bi00579a030
10.1021/bi00345a040
10.1002/j.1460-2075.1983.tb01591.x
10.1038/171964b0
{'key': 'B13', 'first-page': '25', 'volume': '14', 'author': 'Crick FHC', 'year': '1957', 'journal-title': 'Symp. Biochem. Soc.'}
/ Symp. Biochem. Soc. by Crick FHC (1957)10.1073/pnas.43.5.416
10.1016/S0021-9258(19)77302-5
/ J. Biol. Chem. by Hoagland MB (1958)10.1126/science.147.3664.1462
- Pauling L. 1958. InArbeiten aus dem Gebiet der Naturstoffe(Festschr. Prof. Dr. Arthur Stoll Siebzigsten Geburtstag, 8 Jan. 1957), pp.597–602. Basel: Birkhäuser
10.1042/bj0890082
10.1042/bj1281353
10.1016/0092-8674(77)90147-7
10.1016/0047-6374(81)90089-0
10.1073/pnas.51.5.883
10.1016/S0022-2836(64)80163-7
10.1101/SQB.1966.031.01.086
10.1073/pnas.76.7.3174
10.1021/bi00849a020
10.1038/225508a0
10.1073/pnas.65.3.638
10.1038/231126a0
10.1111/j.1432-1033.1973.tb02586.x
10.1016/0006-291X(71)90695-4
10.1016/0022-2836(76)90214-X
10.1080/07391102.1985.10508436
10.1073/pnas.75.2.610
10.1073/pnas.74.1.198
10.1146/annurev.biochem.70.1.415
10.1021/bi9809425
10.1021/bi991186l
10.1006/jmbi.1999.2700
10.1021/bi00359a020
10.1016/0968-0004(87)90146-0
10.1038/358123a0
10.1038/350628a0
10.1073/pnas.87.21.8187
10.1021/bi00108a005
10.1126/science.1373521
10.1021/bi00359a019
10.1021/bi00388a059
10.1021/bi00367a061
10.1016/0006-3002(60)90394-2
10.1016/S0021-9258(18)64320-0
/ J. Biol. Chem. by Lipsett MN (1961)10.1016/S0021-9258(18)91420-1
/ J. Biol. Chem. by Lipsett MN (1964)10.1101/SQB.1966.031.01.078
10.1016/S0079-6603(08)60642-X
10.1073/pnas.51.3.487
10.1101/SQB.1966.031.01.084
- Gorini L. 1974. InRibosomes, ed.M Nomura, A Tissiéres, P Lengyel, pp.791–803. Cold Spring Harbor, NY: Cold Spring Harbor Lab.
10.1038/222333a0
10.1128/jb.121.2.670-674.1975
/ J. Bacteriol. by Chakrabarti S (1975)10.1016/S0079-6603(08)60378-5
10.1126/science.157.3794.1314
10.1016/0022-2836(67)90281-1
10.1016/0022-2836(69)90336-2
10.1016/0022-2836(71)90101-X
10.1073/pnas.68.9.2263
10.1007/BF00267778
10.1007/BF00329777
10.1016/0022-2836(72)90324-5
10.1016/0022-2836(71)90362-7
10.1016/0022-2836(71)90363-9
10.1073/pnas.74.12.5496
10.1038/newbio234261a0
10.1073/pnas.82.3.717
10.1111/j.1432-1033.1986.tb09630.x
10.1007/BF00594747
10.1016/0014-5793(82)80693-5
10.1016/0022-2836(74)90586-5
10.1073/pnas.71.10.4135
10.1016/S0300-9084(75)80139-8
10.1017/S0033583500001669
10.1002/j.1460-2075.1982.tb01240.x
10.1016/S0021-9258(19)69044-7
/ J. Biol. Chem. by Thompson RC (1981)10.1007/BF00328707
10.1016/0968-0004(88)90047-3
10.1073/pnas.79.16.4922
10.1016/S0079-6603(08)60366-9
10.1016/S0021-9258(18)37677-4
/ J. Biol. Chem. by Hausner TP (1988)10.1002/j.1460-2075.1990.tb07904.x
10.1021/bi00206a033
10.1002/j.1460-2075.1995.tb07259.x
10.1093/emboj/17.24.7490
10.1093/emboj/18.13.3800
10.1002/j.1460-2075.1996.tb01066.x
10.1016/0022-2836(92)90986-T
10.1038/365126a0
10.1016/0969-2126(93)90007-4
10.1016/S1097-2765(04)00005-X
10.1073/pnas.69.11.3115
10.1016/0022-2836(90)90016-F
10.1073/pnas.87.3.1042
10.1126/science.285.5434.1722
10.1038/327389a0
10.1038/370659a0
10.1126/science.274.5291.1367
10.1006/jmbi.1997.1551
10.1006/jmbi.1998.2442
10.1038/72364
{'key': 'B108', 'first-page': '428', 'volume': '1', 'author': 'Yonath A', 'year': '1980', 'journal-title': 'Biochem. Int.'}
/ Biochem. Int. by Yonath A (1980)10.1016/0014-5793(87)80838-4
{'key': 'B110', 'first-page': '953', 'volume': '15', 'author': 'Glotz C', 'year': '1987', 'journal-title': 'Biochem. Int.'}
/ Biochem. Int. by Glotz C (1987)10.1016/0022-2836(88)90216-1
10.1016/0022-2836(91)90730-T
10.1107/S010876739800991X
10.1038/23631
10.1126/science.285.5436.2095
10.1016/S0092-8674(00)81455-5
10.1038/23641
10.1038/35030006
10.1126/science.289.5481.905
10.1016/S0092-8674(00)00084-2
10.1006/jmbi.2001.5359
10.1093/emboj/20.8.1829
10.1126/science.1060089
10.1038/35030019
10.1016/S0969-2126(01)00629-3
10.1016/S0969-2126(02)00934-6
10.1126/science.1057766
10.1126/science.1060612
10.1038/86221
10.1073/pnas.081082398
10.1073/pnas.182221799
10.1016/S0092-8674(02)01086-3
10.1126/science.3810156
10.1126/science.3810155
10.1017/S0033583500003644
10.1146/annurev.biophys.31.082901.134202
10.1016/S0021-9258(18)50607-4
/ J. Biol. Chem. by Douglass J (1979)10.1074/jbc.M100017200
10.1038/416281a
10.1038/38770
10.1038/342142a0
10.1016/S0022-2836(05)80023-3
10.1093/emboj/cdf326
{'key': 'B144', 'first-page': '849', 'volume': '9', 'author': 'Stark H', 'year': '2002', 'journal-title': 'Nat. Struct. Biol.'}
/ Nat. Struct. Biol. by Stark H (2002)10.1126/science.270.5241.1464
10.1038/nsb1003
10.1016/S0968-0004(03)00066-5
10.1074/jbc.271.2.646
10.1073/pnas.1133380100
10.1016/0022-2836(76)90243-6
10.1038/226817a0
10.1017/S1355838202027061
10.1016/S0021-9258(19)86519-5
/ J. Biol. Chem. by Yates JL (1979)10.1016/0022-2836(92)90466-W
10.1016/S0300-9084(02)01409-8
10.1038/nsmb742
10.1073/pnas.72.11.4248
10.1128/9781555818333.ch22
10.1093/nar/2.8.1421
10.1016/0022-2836(79)90282-1
10.1016/0022-2836(89)90496-8
10.1016/0022-2836(89)90497-X
10.1006/jmbi.1994.1096
10.1006/jmbi.1994.1095
10.1261/rna.2184703
10.1021/bi992331y
10.1038/250546a0
10.1128/9781555818142.ch28
10.1016/S0079-6603(02)71050-7
10.1074/jbc.270.24.14541
10.1002/j.1460-2075.1990.tb07447.x
10.1006/jmbi.1994.1041
10.1111/j.1432-1033.1991.tb16459.x
10.1016/j.jmb.2003.12.080
10.1073/pnas.54.3.880
10.1074/jbc.270.30.17680
10.1016/S0092-8674(00)00216-6
10.1016/S0021-9258(18)67628-8
/ J. Biol. Chem. by Rheinberger HJ (1986)10.1126/science.277.5330.1262
10.1073/pnas.92.23.10555
10.1017/S1355838200000637
{'key': 'B182', 'volume-title': 'Structural studies of the 30S ribosomal subunit', 'author': 'Carter AP', 'year': '2002'}
/ Structural studies of the 30S ribosomal subunit by Carter AP (2002)10.1261/rna.5172104
10.1093/nar/26.1.148
10.1093/nar/gkh185
10.1021/bi001302g
10.1074/jbc.M200253200
10.1261/rna.5142404
10.1038/nsmb861
10.1073/pnas.69.5.1192
10.1038/newbio242230a0
10.1016/0092-8674(81)90086-6
10.1016/S0968-0004(02)02064-9
10.1038/sj.embor.embor825
10.1016/j.cell.2004.06.012
10.1038/34593
10.1126/science.286.5448.2305
10.1016/S0092-8674(04)00252-1
10.1016/S0092-8674(01)00515-3
10.1038/2925
10.1146/annurev.biochem.71.110601.135453
10.1074/jbc.274.25.17395
10.1016/S0969-2126(99)80017-3
10.1016/S0969-2126(03)00051-0
10.1038/nsmb831
10.1016/S0022-2836(03)00236-5
10.1126/science.1064242
10.1038/171737a0
10.1073/pnas.73.3.804
10.1016/S0300-9084(97)86714-4
Dates
Type | When |
---|---|
Created | 20 years, 5 months ago (Feb. 25, 2005, 10:55 p.m.) |
Deposited | 3 years, 10 months ago (Oct. 5, 2021, 7 a.m.) |
Indexed | 2 weeks ago (Aug. 7, 2025, 4:54 p.m.) |
Issued | 20 years, 2 months ago (June 1, 2005) |
Published | 20 years, 2 months ago (June 1, 2005) |
Published Print | 20 years, 2 months ago (June 1, 2005) |
@article{Ogle_2005, title={STRUCTURAL INSIGHTS INTO TRANSLATIONAL FIDELITY}, volume={74}, ISSN={1545-4509}, url={http://dx.doi.org/10.1146/annurev.biochem.74.061903.155440}, DOI={10.1146/annurev.biochem.74.061903.155440}, number={1}, journal={Annual Review of Biochemistry}, publisher={Annual Reviews}, author={Ogle, James M. and Ramakrishnan, V.}, year={2005}, month=jun, pages={129–177} }