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Structural implications for ribosomal binding of a 2‐thiocytidine modified nucleotide at position 32 of tRNAArg
Author(s) -
Cantara William A,
Kim Jia,
Agris Paul F
Publication year - 2009
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.23.1_supplement.839.1
Subject(s) - transfer rna , 30s , ribosomal rna , circular dichroism , arginine , ribosomal protein , ribosome , translation (biology) , chemistry , biochemistry , computational biology , genetics , biology , stereochemistry , rna , amino acid , gene , messenger rna
Four of the five arginine tRNAs in E. coli contain a conserved 2‐thiocytidine (s 2 C) at position 32. The structural implications of this modification and how it impacts ribosomal binding are key to understanding its role in translation. The hypothesis that s 2 C modification creates specific structural changes in the anticodon stem and loop (ASL) of tRNA Arg that result in functional binding differences is tested herein. Using electophoretic mobility, UV melt, circular dichroism, NMR and filter binding assays, we are able to develop structural and functional profiles of an array of unmodified and s 2 C‐containing arginine ASLs. It is shown that by combining the structural results with binding data creates a comprehensive view of how the complex dynamics of the translational machinery is influenced by the presence of s 2 C at position 32 of ASL Arg . This study is funded by the National Science Foundation.