tRNA is a vital molecule of life and has been a focus of biochemical research since long. New aspects of tRNA biology have been drawn to light recently. Accumulating data indicates that tRNA has many diverse biological functions other than its canonical role in coding for amino acids. tRNA halves are produced by cutting the tRNA molecule from its anti-codon loop by angiognenin and even smaller RNA fragments (tRFs) produced from 5’ or 3’ ends of mature tRNA have been shown to have biological functions, most notable of which is the inhibition of the initiation of protein synthesis. In our study, the aim was to show the interaction between tRFs and RNA binding proteins. For this reason, two proteins were determined: Rox8 and D-La which are Drosophila homologs of human TIA-1 and La. In the beginning of study, we overexpressed FLAG-tagged versions of these proteins in S2 cells. Then immunoprecipitation experiments were performed with the tagged proteins. At the end of our research the potential interaction between tRFs and tRF related proteins are demonstrated.