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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2013
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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.
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Authors Dickerman, Benjamin K;McDonald, Jocelyn A;Sen, Ganes C;
Journal F1000Research
Year 2013
DOI DOI not found
URL
http://f1000research.com/articles/2-220/v1
Keywords
Biology (General) Medicine Technology Pediatrics Science Immunologic diseases. Allergy neurosciences. biological psychiatry. neuropsychiatry neurology. diseases of the nervous system diseases of the musculoskeletal system

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