NMR-based identification of peptides that specifically recognize the d-arm of tRNA

Biochimie. 2005 Sep-Oct;87(9-10):885-8. doi: 10.1016/j.biochi.2005.02.003. Epub 2005 Feb 25.

Abstract

Human tRNA3(Lys) is used by HIV virus as a primer for the reverse transcription of its genome. The 18 nucleotides at the 3'-end of the tRNA3(Lys) are hybridized to a complementary sequence of the viral RNA called the primer-binding site. A screen against the human tRNA3(Lys) over a peptide library designed to target RNA has been performed. Of the 175 hexapeptides tested, three were found to bind to the d-stem of tRNA3(Lys). Alanine-scanning was used to define the determinants of the interaction between the peptides and tRNA3(Lys). They also bind to two other tested tRNAs, also at the level of the d-stem and loop, although the nucleotide sequence of the stem differs in one of them. These short peptides thus recognize specific structural features within the d-stem and loop of tRNAs. Associated with other pharmacophores, they could be useful to design optimized ligands targeting specific tRNAs such as retroviral replication primers.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Binding Sites
  • DNA Primers
  • HIV-1 / genetics
  • Humans
  • Ligands
  • Nuclear Magnetic Resonance, Biomolecular / methods*
  • Nucleic Acid Conformation
  • Peptide Library
  • Peptides / metabolism*
  • RNA, Transfer / antagonists & inhibitors
  • RNA, Transfer / chemistry
  • RNA, Transfer / metabolism*
  • Reverse Transcription

Substances

  • DNA Primers
  • Ligands
  • Peptide Library
  • Peptides
  • RNA, Transfer