Testosterone and its dimers alter tRNA morphology


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Abstract

HIGHLIGHTSThe effect of testosterone and its dimers on tRNA morphology is reported here.Testosterone dimers form stronger conjugates with tRNA than monomer.Hydrophobic contacts are mainly observed in steroid-tRNA adducts.Major tRNA morphological changes were observed with testosterone conjugation.Our study elucidates the nature of steroid-tRNA interactions.The morphology of tRNA was studied upon conjugation with testosterone and its aliphatic and aromatic dimers, using multiple spectroscopic methods, transmission electron microscopy (TEM) and molecular modeling. Structural analysis showed that testosterone binds tRNA through A62, A64, C60, C61, C63, G51, U50 and U59 bases. The binding affinity was testosterone dimer-aromatic > testosterone dimer-aliphatic > testosterone. The steroid loading efficacy was 35–45%. Transmission electron microscopy showed major changes in tRNA morphology upon testosterone interaction with an increase in the diameter of the tRNA aggregate, indicating encapsulation of testosterone by tRNA.

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