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      The RNA World: molecular cooperation at the origins of life.

      Author(s): 1 , 2
      Publication date (Electronic):
      Journal: Nature reviews. Genetics

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          Abstract

          The RNA World concept posits that there was a period of time in primitive Earth's history - about 4 billion years ago - when the primary living substance was RNA or something chemically similar. In the past 50 years, this idea has gone from speculation to a prevailing idea. In this Review, we summarize the key logic behind the RNA World and describe some of the most important recent advances that have been made to support and expand this logic. We also discuss the ways in which molecular cooperation involving RNAs would facilitate the emergence and early evolution of life. The immediate future of RNA World research should be a very dynamic one.

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          Most cited references94

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          Systematic evolution of ligands by exponential enrichment: RNA ligands to bacteriophage T4 DNA polymerase.

          C Tuerk, L Gold (1990)
          High-affinity nucleic acid ligands for a protein were isolated by a procedure that depends on alternate cycles of ligand selection from pools of variant sequences and amplification of the bound species. Multiple rounds exponentially enrich the population for the highest affinity species that can be clonally isolated and characterized. In particular one eight-base region of an RNA that interacts with the T4 DNA polymerase was chosen and randomized. Two different sequences were selected by this procedure from the calculated pool of 65,536 species. One is the wild-type sequence found in the bacteriophage mRNA; one is varied from wild type at four positions. The binding constants of these two RNA's to T4 DNA polymerase are equivalent. These protocols with minimal modification can yield high-affinity ligands for any protein that binds nucleic acids as part of its function; high-affinity ligands could conceivably be developed for any target molecule.
          Article 0 comments Cited 958 times – based on 0 reviews     Review now
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            The origin of the genetic code.

            F.H.C. Crick (1968)
            Article 0 comments Cited 481 times – based on 0 reviews     Review now
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              The structural basis of ribosome activity in peptide bond synthesis.

              P Nissen, J Hansen, N Ban … (2000)
              Using the atomic structures of the large ribosomal subunit from Haloarcula marismortui and its complexes with two substrate analogs, we establish that the ribosome is a ribozyme and address the catalytic properties of its all-RNA active site. Both substrate analogs are contacted exclusively by conserved ribosomal RNA (rRNA) residues from domain V of 23S rRNA; there are no protein side-chain atoms closer than about 18 angstroms to the peptide bond being synthesized. The mechanism of peptide bond synthesis appears to resemble the reverse of the acylation step in serine proteases, with the base of A2486 (A2451 in Escherichia coli) playing the same general base role as histidine-57 in chymotrypsin. The unusual pK(a) (where K(a) is the acid dissociation constant) required for A2486 to perform this function may derive in part from its hydrogen bonding to G2482 (G2447 in E. coli), which also interacts with a buried phosphate that could stabilize unusual tautomers of these two bases. The polypeptide exit tunnel is largely formed by RNA but has significant contributions from proteins L4, L22, and L39e, and its exit is encircled by proteins L19, L22, L23, L24, L29, and L31e.
              Article 0 comments Cited 410 times – based on 0 reviews     Review now
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                Author and article information

                Journal
                Journal ID (iso-abbrev): Nat. Rev. Genet.
                Title: Nature reviews. Genetics
                ISSN (Electronic): 1471-0064
                ISSN (Print): 1471-0056
                Publication date (Electronic): Jan 2015
                Volume: 16
                Issue: 1
                Affiliations
                [1 ] Origins Institute and Department of Physics and Astronomy, McMaster University, Hamilton, Ontario L8S 4M1, Canada.
                [2 ] Department of Chemistry, Portland State University, PO Box 751, Portland, Oregon 97207, USA.
                Article
                Publisher Item ID: nrg3841
                DOI: 10.1038/nrg3841
                PubMed ID: 25385129
                SO-VID: dc3bf572-9d3c-4a75-aee4-e449939bb731
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