The Human dsRNA binding protein PACT is unable to functionally substitute for the Drosophila dsRNA binding protein R2D2 [v1; ref status: indexed, http://f1000r.es/201]

The Human dsRNA binding protein PACT is unable to functionally substitute for the Drosophila dsRNA binding protein R2D2 [v1; ref status: indexed, http://f1000r.es/201]

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The primary function of the dsRNA binding protein (dsRBP) PACT/RAX is to activate the dsRNA dependent protein kinase PKR in response to stress signals.Additionally, it RYE FLAKES ORG has been identified as a component of the small RNA processing pathway.A role for PACT/RAX in this pathway represents an important interplay between two modes of post-transcriptional gene regulation.The function of PACT/RAX in this context is poorly understood.

Thus, additional models are required to clarify Accessories the mechanism by which PACT/RAX functions.In this study, Drosophila melanogaster was employed to identify functionally orthologous dsRNA-binding proteins.Transgenic Drosophila expressing human PACT were generated to determine whether PACT is capable of functionally substituting for the Drosophila dsRBP R2D2, which has a well-defined role in small RNA biogenesis.Results presented here indicate that PACT is unable to substitute for R2D2 at the whole organism level.