Collect. Czech. Chem. Commun. 1998, 63, 842-850

Interaction of HIV Tat Peptides With tRNAPhe from Yeast

Iwona Buskiewicza, Malgorzata Giel-Pietraszuka, Piotr Muchab, Piotr Rekowskib, Gotfryd Kupryszewskib and Miroslawa Z. Barciszewskaa

a Institute of Bioorganic Chemistry, Polish Academy of Sciences, Noskowskiego 12/14, 61-704 Poznań, Poland
b Faculty of Chemistry, University of Gdansk, Sobieskiego 18, 80-952 Gdansk, Poland


We present data on the interaction of arginine-rich peptides of human immunodeficiency virus (HIV-Tat) with tRNAPhe of Saccharomyces cerevisiae. We have found that tRNA forms complexes with the Tat1 peptide of amino acid sequence GRKKRRQRRRA and its mutants where R is replaced by D-arginine, citrulline or ornithine. The structure of tRNA-Tat1 complex was probed by specific RNases digestions and Pb2+-induced cleavage of phosphodiester bond of guanosine. The nucleotide sequence UGGG located in the dihydrouridine loop of tRNAPhe binds to Tat peptide and therefore is specifically protected against RNases and is not hydrolyzed by Pb2+ ion. It seems that the peptide-RNA complex formation depends on direct recognition of guanine moieties of tRNA with arginine residues. These interactions are similar to those observed in many DNA-protein complexes, but are different from those previously observed for TAR RNA-Tat complexes.

Keywords: Tat peptides; TAR RNA; tRNAPhe; Protein-nucleic acids interactions; HIV.