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Continuous in vitro evolution of a ribozyme that catalyzes three successive nucleotidyl addition reactions

Academic Article
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Overview

related to degree

  • McGinness, Kathleen, Ph.D. in Chemistry, Scripps Research 1996 - 2001

authors

  • McGinness, Kathleen
  • Wright, M. C.
  • Joyce, Gerald

publication date

  • May 2002

journal

  • Chemistry & Biology  Journal

abstract

  • Variants of the class I ligase ribozyme, which catalyzes joining of the 3' end of a template bound oligonucleotide to its own 5' end, have been made to evolve in a continuous manner by a simple serial transfer procedure that can be carried out indefinitely. This process was expanded to allow the evolution of ribozymes that catalyze three successive nucleotidyl addition reactions, two template-directed mononucleotide additions followed by RNA ligation. During the development of this behavior, a population of ribozymes was maintained against an overall dilution of more than 10(406). The resulting ribozymes were capable of catalyzing the three-step reaction pathway, with nucleotide addition occurring in either a 5'-->3' or a 3'-->5' direction. This purely chemical system provides a functional model of a multi-step reaction pathway that is undergoing Darwinian evolution.

subject areas

  • Base Sequence
  • Catalysis
  • DNA-Directed RNA Polymerases
  • Evolution, Molecular
  • Kinetics
  • Molecular Sequence Data
  • Mutagenesis
  • Nucleic Acid Conformation
  • Nucleotides
  • Phosphorus Radioisotopes
  • Polymerase Chain Reaction
  • Promoter Regions, Genetic
  • RNA Ligase (ATP)
  • RNA, Catalytic
  • Sequence Analysis, RNA
  • Substrate Specificity
  • Viral Proteins
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Identity

International Standard Serial Number (ISSN)

  • 1074-5521

Digital Object Identifier (DOI)

  • 10.1016/s1074-5521(02)00136-9

PubMed ID

  • 12031665
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Additional Document Info

start page

  • 585

end page

  • 596

volume

  • 9

issue

  • 5

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