Evolution of Protein Synthesis from an RNA World
Open accessAbstract
Because of the molecular complexity of the ribosome and protein synthesis, it is a challenge to imagine how translation could have evolved from a primitive RNA World.Two specific suggestions are made here to help to address this, involving separate evolution of the peptidyl transferase and decoding functions.First, it is proposed that translation originally arose not to synthesize functional proteins, but to provide simple ( perhaps random) peptides that bound to RNA, increasing its available structure space, and therefore its functional capabilities.Second, it is proposed that the decoding site of the ribosome evolved from a mechanism for duplication of RNA.This process involved homodimeric "duplicator RNAs," resembling the anticodon arms of tRNAs, which directed ligation of trinucleotides in response to an RNA template.Outline 1 Introduction 2 Translation out of an RNA World 3 Peptidyl transferase: the ribosome is a ribozyme 4 Aminoacyl-tRNA selection: the 30S subunit a site 5 The 30S subunit p site: another function of rRNA 6 RNA molecular mechanics and translocation 7 What are ribosomal proteins for?8 "Stop tRNAs" and the evolution of type I release factors 9 dRNA and the origins of the ribosomal decoding site 10 The driving force for evolution of translation from an RNA world 11
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
Given genes and proteins, the origin of molecular machines such as the ATPase is an impressive but not conceptually challenging evolutionary step, far less problematic than the hurdles at the origin of the ribosome and the code.
“Given genes and proteins, the origin of molecular machines such as the ATPase is an admittedly impressive, but not conceptually challenging, evolutionary step; it is a far less problematic increment than the hurdles that had to be surmounted at the origin of the ribosome and the code [110,117].”
From Early bioenergetic evolution (2013) · cites this paper as [117]
The Introduction (page unavailable) calls the origin of the ribosome one of the most challenging problems in molecular evolution, and the Conclusions (page unavailable) say that the evolution of coding remains the most difficult step to explain. The paper does not address the origin of ATPase or say that, given genes and proteins, molecular machines are comparatively easy to evolve. (LLM, conf=0.86)
Experimental — accuracy not yet measuredThe inferred oldest core of the ribosome consists of a few surprisingly simple sequences.
“Indeed, the ribosome can be thought of as essentially an entropy ‘trap’ for carefully aligned substrates [199], and the inferred oldest core of the ribosome consists of a few surprisingly simple sequences [200].”
From The RNA world as a model system to study the origin of life (2015) · cites this paper as [200]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Cites
Principles of Nucleic Acid Structure
Neidle, S., & Sanderson, M. (2008) · Elsevier eBooks · doi:10.1016/b978-0-12-369507-9.x5001-8 · Cited by 4,519 · see citing works
Shine, J., & Dalgarno, L. (1974) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.71.4.1342 · Cited by 3,628 · see citing works
The Complete Atomic Structure of the Large Ribosomal Subunit at 2.4 Å Resolution
Ban, N., Nissen, P., Hansen, J., Moore, P. B., & Steitz, T. A. (2000) · Science · doi:10.1126/science.289.5481.905 · Cited by 3,327 · see citing works
The RNA moiety of ribonuclease P is the catalytic subunit of the enzyme
Guerrier-Takada, C., Gardiner, K., Marsh, T., Pace, N., & Altman, S. (1983) · Cell · doi:10.1016/0092-8674(83)90117-4 · Cited by 2,684 · see citing works
The origin of the genetic code
Crick, F. H. C. (1968) · Journal of Molecular Biology · doi:10.1016/0022-2836(68)90392-6 · Cited by 2,320 · see citing works
The Structural Basis of Ribosome Activity in Peptide Bond Synthesis
Nissen, P., Hansen, J., Ban, N., Moore, P. B., & Steitz, T. A. (2000) · Science · doi:10.1126/science.289.5481.920 · Cited by 2,269 · see citing works
Structure of the 30S ribosomal subunit
Wimberly, B. T., Brodersen, D. E., Clemons, W. M., Morgan-Warren, R. J., Carter, A. P., Vonrhein, C., Hartsch, T., & Ramakrishnan, V. (2000) · Nature · doi:10.1038/35030006 · Cited by 2,035 · see citing works
Crystal structure of the ribosome at 5.5 Å resolution
Yusupov, M. M., Yusupova, G. Z., Baucom, A., Lieberman, K., Earnest, T. N., Cate, J. H. D., & Noller, H. F. (2001) · Science · doi:10.1126/science.1060089 · Cited by 1,944 · see citing works
Self-citationCarter, A. P., Clemons, W. M., Brodersen, D. E., Morgan-Warren, R. J., Wimberly, B. T., & Ramakrishnan, V. (2000) · Nature · doi:10.1038/35030019 · Cited by 1,615 · see citing works
Principles of Nucleic Acid Structure
Parish, J. (1985) · Biochemical Education · doi:10.1016/0307-4412(85)90046-9 · Cited by 1,496 · see citing works
RNA Codewords and Protein Synthesis
Nirenberg, M. W., & Leder, P. (1964) · Science · doi:10.1126/science.145.3639.1399 · Cited by 1,418 · see citing works
Structure of the 70S Ribosome Complexed with mRNA and tRNA
Selmer, M., Dunham, C., Murphy, F., Weixlbaumer, A., Petry, S., Kelley, A. C., Weir, J., & Ramakrishnan, V. (2006) · Science · doi:10.1126/science.1131127 · Cited by 1,352 · see citing works
Recognition of Cognate Transfer RNA by the 30 <i>S</i> Ribosomal Subunit
Ogle, J. M., Brodersen, D. E., Clemons, W. M., Tarry, M. J., Carter, A. P., & Ramakrishnan, V. (2001) · Science · doi:10.1126/science.1060612 · Cited by 1,162 · see citing works
Evolution of the genetic apparatus
Orgel, L. E. (1968) · Journal of Molecular Biology · doi:10.1016/0022-2836(68)90393-8 · Cited by 996 · see citing works
Structure of Functionally Activated Small Ribosomal Subunit at 3.3 Å Resolution
Schluenzen, F., Tocilj, A., Zarivach, R., Harms, J., Gluehmann, M., Janell, D., Bashan, A., Bartels, H., Agmon, I., Franceschi, F., et al. (2000) · Cell · doi:10.1016/s0092-8674(00)00084-2 · Cited by 979 · see citing works
Gene regulation by riboswitches
Mandal, M., & Breaker, R. R. (2004) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1403 · Cited by 913 · see citing works
A ratchet-like inter-subunit reorganization of the ribosome during translocation
Frank, J., & Agrawal, R. K. (2000) · Nature · doi:10.1038/35018597 · Cited by 799 · see citing works
Unusual Resistance of Peptidyl Transferase to Protein Extraction Procedures
Noller, H. F., Hoffarth, V., & Zimniak, L. (1992) · Science · doi:10.1126/science.1604315 · Cited by 728 · see citing works
Self-citationSTEITZ, J. A., & Jakes, K. S. (1975) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.72.12.4734 · Cited by 692 · see citing works
Riboswitches and the RNA WorldPreprint
Breaker, R. R. (2010) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a003566 · Cited by 679 · see citing works
RNA tertiary interactions in the large ribosomal subunit: The A-minor motif
Nissen, P., Ippolito, J. A., Ban, N., Moore, P. B., & Steitz, T. A. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.081082398 · Cited by 659 · see citing works
α Helix-RNA Major Groove Recognition in an HIV-1 Rev Peptide-RRE RNA Complex
Battiste, J. L., Mao, H., Rao, N. S., Tan, R., Muhandiram, D. R., Kay, L. E., Frankel, A. D., & Williamson, J. R. (1996) · Science · doi:10.1126/science.273.5281.1547 · Cited by 596 · see citing works
Conformation of the TAR RNA-Arginine Complex by NMR Spectroscopy
Puglisi, J. D., Tan, R., Calnan, B. J., Frankel, A. D., & Williamson, J. R. (1992) · Science · doi:10.1126/science.1621097 · Cited by 596 · see citing works
Serganov, A., Yuan, Y.-R., Pikovskaya, O., Polonskaia, A., Malinina, L. V., Phan, A. T., Höbartner, C., Micura, R., Breaker, R. R., & Patel, D. J. (2004) · Chemistry & Biology · doi:10.1016/j.chembiol.2004.11.018 · Cited by 560 · see citing works
The Ribosome : structure, function, and evolution
Hill, W. E. (1990) · Medical Entomology and Zoology · Cited by 522 · see citing works
Interaction of tRNA with 23S rRNA in the ribosomal A, P, and E sites
Moazed, D., & Noller, H. F. (1989) · Cell · doi:10.1016/0092-8674(89)90128-1 · Cited by 500 · see citing works
Self-citationTransfer RNA shields specific nucleotides in 16S ribosomal RNA from attack by chemical probes
Moazed, D., & Noller, H. F. (1986) · Cell · doi:10.1016/0092-8674(86)90813-5 · Cited by 420 · see citing works
Self-citationAn operational RNA code for amino acids and possible relationship to genetic code.
SCHIMMEL, P. R., Giegé, R., Moras, D., & Yokoyama, S. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.19.8763 · Cited by 418 · see citing works
Spontaneous Intersubunit Rotation in Single Ribosomes
Cornish, P. V., Ermolenko, D. N., Noller, H. F., & Ha, T. (2008) · Molecular Cell · doi:10.1016/j.molcel.2008.05.004 · Cited by 393 · see citing works
Self-citationOchoa, S. (2015) · KARGER eBooks · doi:10.1159/000428951 · Cited by 370 · see citing works
Structural basis for translation termination on the 70S ribosome
Laurberg, M., Asahara, H., Korostelev, A. A., Zhu, J., Trakhanov, S. D., & Noller, H. F. (2008) · Nature · doi:10.1038/nature07115 · Cited by 357 · see citing works
Self-citationAn 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. (2005) · Nature · doi:10.1038/nature04152 · Cited by 351 · see citing works
Solution Structure of a Bovine Immunodeficiency Virus Tat-TAR Peptide-RNA Complex
Puglisi, J. D., Chen, L., Blanchard, S. C., & Frankel, A. D. (1995) · Science · doi:10.1126/science.270.5239.1200 · Cited by 339 · see citing works
Moazed, D., & Noller, H. F. (1987) · Biochimie · doi:10.1016/0300-9084(87)90215-x · Cited by 338 · see citing works
Self-citationStructure of Functionally Activated Small Ribosomal Subunit
Schluenzen, F., Tocilj, A., Zarivach, R., et al. (2000) · Cited by 331 · see citing works
Insights into Translational Termination from the Structure of RF2 Bound to the Ribosome
Weixlbaumer, A., Jin, H. R., Neubauer, C., et al. (2008) · Science · doi:10.1126/science.1164840 · Cited by 308 · see citing works
Endo, Y., & Wool, I. G. (1982) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)34241-8 · Cited by 304 · see citing works
Peptide bond formation by in vitro selected ribozymes
Zhang, B., & Cech, T. R. (1997) · Nature · doi:10.1038/36375 · Cited by 299 · see citing works
The genetic code : the molecular basis for genetic expression
Woese, C. R. (1967) · Harper & Row eBooks · Cited by 295 · see citing works
Moazed, D., & Noller, H. F. (1990) · Journal of Molecular Biology · doi:10.1016/0022-2836(90)90016-f · Cited by 292 · see citing works
Self-citationRNA-Protein Interactions in 30 S Ribosomal Subunits: Folding and Function of 16 S rRNA
Stern, S., Powers, T., Changchien, L., & Noller, H. F. (1989) · Science · doi:10.1126/science.2658053 · Cited by 285 · see citing works
Self-citationCatalysis of peptide bond formation by 50 s ribosomal subunits from Escherichia coli
Monro, R. E. (1967) · Journal of Molecular Biology · doi:10.1016/0022-2836(67)90271-9 · Cited by 276 · see citing works
Poole, A. M., Jeffares, D. C., & Penny, D. (1998) · Journal of Molecular Evolution · doi:10.1007/pl00006275 · Cited by 274 · see citing works
Mechanism of Kasugamycin Resistance in Escherichia coli
Helser, T. L., DAVIES, J. E., & Dahlberg, J. E. (1972) · Nature New Biology · doi:10.1038/newbio235006a0 · Cited by 270 · see citing works
Gavrilova, L. P., Oe, K., Koteliansky, V., Nm, R., & Spirin, A. S. (1976) · Journal of Molecular Biology · doi:10.1016/0022-2836(76)90243-6 · Cited by 258 · see citing works
Crystal structure of a translation termination complex formed with release factor RF2
Korostelev, A. A., Asahara, H., Lancaster, L., Laurberg, M., Hirschi, A., Zhu, J., Trakhanov, S. D., Scott, W. G., & Noller, H. F. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0810953105 · Cited by 254 · see citing works
Self-citationSharp, P. A. (1991) · Science · doi:10.1126/science.1948046 · Cited by 251 · see citing works
Specific Inactivation of 16S Ribosomal RNA Induced by Colicin E3 In Vivo
Bowman, C. M., Dahlberg, J. E., Ikemura, T., et al. (1971) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.68.5.964 · Cited by 243 · see citing works
Recognition of the Codon-Anticodon Helix by Ribosomal RNA
Yoshizawa, S., Fourmy, D., & Puglisi, J. D. (1999) · Science · doi:10.1126/science.285.5434.1722 · Cited by 237 · see citing works
A hierarchical model for evolution of 23S ribosomal RNA
Bokov, K., & Steinberg, S. V. (2009) · Nature · doi:10.1038/nature07749 · Cited by 228 · see citing works
Role of the Protein Moiety of Ribonuclease P, a Ribonucleoprotein Enzyme
Reich, C. I., Olsen, G. J., Pace, B., & Pace, N. R. (1988) · Science · doi:10.1126/science.3122322 · Cited by 225 · see citing works
Conservation of primary structure in 16S ribosomal RNA
Woese, C., Fox, G., Zablen, L., Uchida, T., Bonen, L., Pechman, K. R., Lewis, B. J., & Stahl, D. (1975) · Nature · doi:10.1038/254083a0 · Cited by 213 · see citing works
The process of mRNA–tRNA translocation
Frank, J., Gao, H., Sengupta, J., et al. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0708517104 · Cited by 206 · see citing works
Prince, J. B., Taylor, B. H., Thurlow, D. L., et al. (1982) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.79.18.5450 · Cited by 205 · see citing works
Structure and Function of Ribosomes and Their Molecular ComponentsPreprint
Nomura, M., Mizushima, S.-I., Ozaki, M., Traub, P., & Lowry, C. V. (1969) · Cold Spring Harbor Symposia on Quantitative Biology · doi:10.1101/sqb.1969.034.01.009 · Cited by 204 · see citing works
Solution structure of an ATP-binding RNA aptamer reveals a novel fold.
Dieckmann, T., Suzuki, E., Nakamura, G. K., & Feigon, J. F. (1996) · Europe PMC (PubMed Central) · Cited by 197 · see citing works
Ribozyme-catalyzed tRNA aminoacylation
Lee (2000) · Nature Structural Biology · doi:10.1038/71225 · Cited by 191 · see citing works
Following movement of the L1 stalk between three functional states in single ribosomes
Cornish, P. V., Ermolenko, D. N., Staple, D. W., Hoang, L., Hickerson, R. P., Noller, H. F., & Ha, T. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0813180106 · Cited by 186 · see citing works
Self-citationStudies on the Formation of Transfer Ribonucleic Acid-Ribosome Complexes
Pestka, S. (1968) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)93445-9 · Cited by 171 · see citing works
Effect of Colicin E3 upon the 30S Ribosomal Subunit of Escherichia coli
Senior, B. W., & Holland, I. B. (1971) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.68.5.959 · Cited by 170 · see citing works
Studies on the formation of transfer ribonucleic acid-ribosome complexes
Pestka, S. (1970) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(70)90329-2 · Cited by 165 · see citing works
Sites of interaction of the CCA end of peptidyl-tRNA with 23S rRNA.
Moazed, D., & Noller, H. F. (1991) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.88.9.3725 · Cited by 143 · see citing works
Self-citationIdentification of a site on 23S ribosomal RNA located at the peptidyl transferase center.
Barta, A., Steiner, G. E., Brosius, J., et al. (1984) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.81.12.3607 · Cited by 142 · see citing works
Intersubunit movement is required for ribosomal translocation
Horan, L. H., & Noller, H. F. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0700762104 · Cited by 141 · see citing works
Self-citationMinimal set of ribosomal components for reconstitution of the peptidyltransferase activity.
Schulze, H., & Nierhaus, K. H. (1982) · The EMBO Journal · doi:10.1002/j.1460-2075.1982.tb01216.x · Cited by 140 · see citing works
Dominant lethal mutations in a conserved loop in 16S rRNA.
Powers, T., & Noller, H. F. (1990) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.87.3.1042 · Cited by 138 · see citing works
Self-citationCatalysis of Ribosomal Translocation by Sparsomycin
Fredrick, K., & Noller, H. (2003) · Science · doi:10.1126/science.1084571 · Cited by 138 · see citing works
Self-citationFunctional Modification of 16S Ribosomal RNA by Kethoxal
Noller, H. F., & Chaires, J. B. (1972) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.69.11.3115 · Cited by 124 · see citing works
Self-citationRNA-Catalyzed Amino Acid Activation
Kumar, R. K., & Yarus, M. (2001) · Biochemistry · doi:10.1021/bi010710x · Cited by 121 · see citing works
Ribosomal Translocation: Facts and Models
Spirin, A. S. (1985) · Progress in nucleic acid research and molecular biology · doi:10.1016/s0079-6603(08)60346-3 · Cited by 114 · see citing works
Affinities of tRNA binding sites of ribosomes from Escherichia coli
Lill, R., Robertson, J. M., & Wintermeyer, W. (1986) · Biochemistry · doi:10.1021/bi00359a025 · Cited by 114 · see citing works
THE GENETICS OF BACTERIAL RIBOSOMES
Davies, J., & Nomura, M. (1972) · Annual Review of Genetics · doi:10.1146/annurev.ge.06.120172.001223 · Cited by 112 · see citing works
EF‐G‐catalyzed translocation of anticodon stem–loop analogs of transfer RNA in the ribosome
Joseph, S., & Noller, H. F. (1998) · The EMBO Journal · doi:10.1093/emboj/17.12.3478 · Cited by 106 · see citing works
Self-citationHydrolysis of fMet-tRNA by Peptidyl Transferase
Caskey, C. T., Beaudet, A. L., Scolnick, E. M., et al. (1971) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.68.12.3163 · Cited by 105 · see citing works
Identification of Bases in 16 S rRNA Essential for tRNA Binding at the 30 S Ribosomal P Site
von Ahsen, U., & Noller, H. F. (1995) · Science · doi:10.1126/science.7528943 · Cited by 98 · see citing works
Self-citationThe driving force for molecular evolution of translation
NOLLER, H. F. (2004) · RNA · doi:10.1261/rna.7142404 · Cited by 96 · see citing works
Self-citationIdentification of a ribosomal protein essential for peptidyl transferase activity.
Moore, V. G., Atchison, R. E., Thomas, G., et al. (1975) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.72.3.844 · Cited by 96 · see citing works
The Roles of RNA in the Synthesis of ProteinPreprint
Moore, P. B., & Steitz, T. A. (2010) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a003780 · Cited by 85 · see citing works
Creating ribosomes with an all-RNA 30S subunit P site
Hoang, L., Fredrick, K., & Noller, H. F. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0405227101 · Cited by 84 · see citing works
Self-citationProtein and Mg2+-induced conformational changes in the S15 binding site of 16 s ribosomal RNA
Orr, J. W., Hagerman, P. J., & Williamson, J. R. (1998) · Journal of Molecular Biology · doi:10.1006/jmbi.1997.1489 · Cited by 83 · see citing works
Specific, rapid synthesis of Phe-RNA by RNA
Illangasekare, M., & Yarus, M. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.10.5470 · Cited by 75 · see citing works
SCHIMMEL, P. R., & Henderson, B. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.24.11283 · Cited by 72 · see citing works
Binding of yeast tRNAphe anticodon arm to Escherichia coli 30 S ribosomes
Rose, S. J., Lowary, P. T., & Uhlenbeck, O. C. (1983) · Journal of Molecular Biology · doi:10.1016/s0022-2836(83)80036-9 · Cited by 58 · see citing works
Jiang, F., Gorin, A. A., Hu, W., Majumdar, A. K., Baskerville, S., Xu, W., Ellington, A. D., & Patel, D. J. (1999) · Structure · doi:10.1016/s0969-2126(00)88337-9 · Cited by 50 · see citing works
Southworth, D. R., Brunelle, J. L., & Green, R. (2002) · Journal of Molecular Biology · doi:10.1016/s0022-2836(02)01196-8 · Cited by 47 · see citing works
Maizels, N., & Weiner, A. M. (1993) · doi:10.1101/087969380.24.577 · Cited by 47 · see citing works
Mutant Studies on the Prokaryotic Ribosome
Dabbs, E. R. (1986) · Springer series in molecular biology · doi:10.1007/978-1-4612-4884-2_43 · Cited by 43 · see citing works
A ratchet-like inter-subunit reorganization of the ribosome during translocation
Frank, J., & Agrawal, R. K. (2018) · WORLD SCIENTIFIC eBooks · doi:10.1142/9789813234864_0025 · Cited by 37 · see citing works
6 On the Origin of the Ribosome: Coevolution of Subdomains of tRNA and rRNA
Noller, H. F. (1993) · doi:10.1101/087969380.24.137 · Cited by 30 · see citing works
Self-citationA Model of the tRNA Binding Sites on the Escherichia Coli Ribosome
Wower, J., Sylvers, L. A., Rosen, K. V., et al. (1993) · Springer eBooks · doi:10.1007/978-1-4615-2407-6_43 · Cited by 27 · see citing works
8 On the Origin of the Ribosome: Coevolution of Subdomains of tRNA and rRNAPreprint
Noller, H. F. (1999) · Cold Spring Harbor Monograph Archive · doi:10.1101/087969589.37.197 · Cited by 24 · see citing works
Self-citationFollowing Movement of the L1 Stalk between Three Functional States in Single Ribosomes
Ermolenko, D. N., Cornish, P. V., Staple, D. W., et al. (2010) · Biophysical Journal · doi:10.1016/j.bpj.2009.12.1420 · Cited by 13 · see citing works
Studies on the formation of transfer ribonucleic acid-ribosome complexes
Chen, B. P., & Pestka, S. (1972) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(72)90127-0 · Cited by 9 · see citing works
The process of mRNA–tRNA translocation
Frank, J., Gao, H., Sengupta, J., et al. (2018) · WORLD SCIENTIFIC eBooks · doi:10.1142/9789813234864_0040 · Cited by 9 · see citing works
Flagged first, then by citations
Research works printed but not linked: 1
- Hill, A. Dahlberg, RA. Garrett, PB. Moore, D. Schlessinger, JR. Warner), pp. 73-92. American Society of Microbiology, Washington, D.C.
Cited by
Sorted by citations
The Origin of Life—Out of the Blue
Sutherland, J. D. (2016) · Angewandte Chemie International Edition · doi:10.1002/anie.201506585 · Cited by 401 · see citing works
Sousa, F. L., Thiergart, T., Landan, G., Nelson-Sathi, S., Pereira, I. A. C., Allen, J. F., Lane, N., & Martin, W. F. (2013) · Philosophical Transactions of the Royal Society B: Biological Sciences · doi:10.1098/rstb.2013.0088 · Cited by 286 · see citing works
“Given genes and proteins, the origin of molecular machines such as the ATPase is an admittedly impressive, but not conceptually challenging, evolutionary step; it is a far less problematic increment than the hurdles that had to be surmounted at the origin of the ribosome and the code [110,117].”
BackgroundThe RNA world as a model system to study the origin of life
Pressman, A., Blanco, C., & Chen, I. A. (2015) · Current Biology · doi:10.1016/j.cub.2015.06.016 · Cited by 225 · see citing works
Root of the Tree: The Significance, Evolution, and Origins of the Ribosome
Bowman, J. C., Petrov, A. S., Frenkel-Pinter, M., Penev, P. I., & Williams, L. D. (2020) · Chemical Reviews · doi:10.1021/acs.chemrev.9b00742 · Cited by 197 · see citing works
Ribozyme-catalysed RNA synthesis using triplet building blocks
Attwater, J., Raguram, A., Morgunov, A. S., Gianni, E., & Holliger, P. (2018) · eLife · doi:10.7554/elife.35255 · Cited by 147 · see citing works
Camprubí, E., de Leeuw, J. W., House, C. H., Raulin, F., Russell, M. J., Spang, A., Tirumalai, M. R., & Westall, F. (2019) · Space Science Reviews · doi:10.1007/s11214-019-0624-8 · Cited by 84 · see citing works
“The ribosome thus, links the genotype and phenotype (Noller 2012) and represents a universal molecular fossil with multiple layers of ‘chronologically’ separable domains (Bokov and Steinberg 2009; Hsiao et al. 2013b; Petrov et al. 2014a, b; Petrov et al. 2015; Lanier et al. 2016; Bernier et al.…”
BackgroundChatterjee, S., & Yadav, S. (2019) · Life · doi:10.3390/life9010025 · Cited by 80 · see citing works
“Central to the development of ribosomes are RNAs that spawn the tRNAs, and a symmetrical region that is deep within the large ribosomal RNA, where the peptidyl transferase reaction occurs [77,89,90].”
BackgroundKunnev, D., & Gospodinov, A. (2018) · Life · doi:10.3390/life8040044 · Cited by 24 · see citing works
- Authors
- Noller, H. F.
- Affiliations
- University of California, Santa Cruz (US)
- Corresponding author
- Noller, H. F.
- ORCID
- Noller, H. F.
- Venue
- Cold Spring Harbor Perspectives in Biology
- Publisher
- Cold Spring Harbor Laboratory
- Published
- 2010-07-07
- Volume
- 4
- Issue
- 4
- Pages
- a003681-a003681
- ISSN
- 1943-0264 (ISSN-L)
- PMC
- PMC3312679
- OpenAlex
- W2137913279
- Cited by
- 155
- References
- 95
- Citations by year
- 2026: 8 · 2025: 15 · 2024: 20 · 2023: 8 · 2022: 10 · 2021: 11 · 2020: 14 · 2019: 10 · 2018: 10 · 2017: 7 · 2016: 4 · 2015: 7 · 2014: 10 · 2013: 8 · 2012: 2
- Type
- posted content
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Cold Spring Harbor Perspectives in Biology (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Science Foundation
- W. M. Keck Foundation
- National Institutes of Health
- National Institute of General Medical Sciences (R01GM017129)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA and protein synthesis mechanisms
- Physical Sciences › Physics and Astronomy › Astronomy and Astrophysics › Origins and Evolution of Life
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Evolution and Genetic Dynamics
- Keywords
- origin of translation, RNA world, ribosome evolution, peptidyl transferase, ribozymes, ribosomal decoding site, aminoacyl-tRNA selection, 30S subunit, ribosomal proteins, anticodon, ribosome translocation, protein synthesis
- MeSH terms
- Biological Evolution, Nucleic Acid Conformation, RNA, Protein Biosynthesis
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
