Paul F Agris

  • Kristen Corbosiero


    Dr. Agris’ group is interested in understanding the chemistry and structure of codon recognition, particularly in regard to the ubiquitous posttranscriptional modifications of tRNA’s anticodon. The findings from Dr. Agris’s laboratory have altered our understanding of the Wobble Hypothesis to include the vast majority of modified nucleosides. The work continues with the study of modified nucleoside importance to the decoding of those codons rarely used and thus, able to control the extent of mRNA translation. More recently, this research has revealed how keto-enol and amine-imine tautomerism of modified nucleosides controls codon recognition, and how a modification two nucleosides remote from the anticodon of tRNA regulates wobble codon recognition.

    Dr. Agris’ group uses a comprehensive approach of molecular/cell biology, biochemistry and structural biology (NMR and crystallography) to reveal the structure/function relationships of RNA and RNA interactions. An understanding of chemistry/structure/function relationships has now evolved to the study of modification-dependent protein and small molecule recognition of RNAs. Using phage display peptide libraries in vitro, and newly developed search algorithms in silico, Dr. Agris has developed 15-amino acid peptides with high affinity and specificity for modified RNAs. These peptides become tools for probing protein recognition of modified nucleosides in protein synthesis, viral and bacterial replication. The peptides and small molecules are also putative therapeutics with extraordinary specificity for their RNA targets in viral and bacterial infections.