Small RNAs are involved in the regulation of different processes in eukaryotes co-transcriptionally or post-transcriptionally. They regulate protein coding genes, influence chromosome biology, transcription, cell development and maintaining genomic integrity. TRIM-NHL family are highly conserved proteins that interact with mRNA through RISC to regulate developmental pathways and cell differentiation in Eukaryotes. The TRIM-NHL family consists of three domains: RING, B-Box and Coiled Coil domains in association with NHL motifs. This combination of domains enables TRIM-NHL proteins to modulate gene expression in various ways such as the ubiquitination of protein targets via the RING domain, as well as mRNA stability via the NHL domain.NHL-2, one of the five members of TRIM-NHL family proteins, in C. elegans functions as a miRNA and endo-siRNA cofactor. NHL-2 showing different functions as co-factor of endogenous siRNA pathway when selectively interact withCSR-1 orWAGO-1. I make extra chromosomal arrays by microinjecting of plasmid constructs, in different genetic backgrounds of worms and analyze the different phenotypes of the rescue mutant. Loss of function of the transgenes in a similar manner to nhl-2, would suggest the role of the mentioned mutant domains. In addition, we looked at P-bodies and NHL-2 GFP protein with RING domain and / or RNA binding domain mutations. As the functional NHL-2 as a part of RISC is expected to be accumulated into p-bodies. Our analysis showed that P-bodies in NHL domain mutations are bigger in size and more in numbers compared to RING domain mutation and full-length NHL-2 injected in nhl-2 null background animals. Indicate that mRNAs are accumulated in P-bodies in absence of RNA binding domain of NHL-2 protein. Decline in mRNA degradation shows RNA binding domain is more functional and critical in the protein of interest.