Effects of complementary loop composition in truncated R3C ligase ribozymes on kiss switch activation

Biosystems. 2019 Mar:177:9-15. doi: 10.1016/j.biosystems.2019.01.004. Epub 2019 Jan 11.

Abstract

The formation of a kissing-loop through the introduction of complementary 7-membered loops is known to dramatically increase the activity of truncated R3C ligase ribozymes that otherwise display reduced activity. Restoration of activity is thought to result from kissing complex formation-induced rearrangement of two molecules with complementary loops. By combining two types of R3C ligase ribozyme mutants, <A> and <hairpin-ΔU>, the influence of loop composition on ligation activity was investigated. Substrate ligation occurred in <hairpin-ΔU>, but not in <A>, despite the absence of a substrate-binding site in <hairpin-ΔU>. Loop-loop interactions of <A>- and <hairpin-ΔU>-variants with complementary 6-membered loops also resulted in proper kissing-complex formation-induced substrate ligation. However, heterogeneous combinations of 7- and 6-membered loops, and/or of 6- and 5-membered loops had distinct results that depended upon the sequence and bulged nucleotides of the loop regions. These differences suggest that both thermodynamic and kinetic controls act upon the kissing-loop interaction-mediated rearrangement of the shortened trans-R3C ribozymes.

Keywords: Activity; Kissing-loop interaction; R3C ligase ribozyme; RNA; RNA world.

MeSH terms

  • Base Pairing
  • Base Sequence
  • Binding Sites
  • Catalytic Domain
  • Kinetics
  • Mutation*
  • Nucleic Acid Conformation
  • Polynucleotide Ligases / chemistry*
  • Polynucleotide Ligases / genetics
  • Polynucleotide Ligases / metabolism*
  • RNA / chemistry*
  • RNA / genetics
  • RNA / metabolism*
  • RNA, Catalytic / chemistry*
  • RNA, Catalytic / genetics
  • RNA, Catalytic / metabolism*
  • Thermodynamics

Substances

  • RNA, Catalytic
  • RNA
  • Polynucleotide Ligases
  • R3C ligase