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]
2046-1402
Abstract
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 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 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.