The Human dsRNA binding protein PACT is unable to functionally substitute for the Drosophila dsRNA binding protein R2D2

The Human dsRNA binding protein PACT is unable to functionally substitute for the Drosophila dsRNA binding protein R2D2

The dsRNA binding protein (dsRBP) PACT was first described as an activator of 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 in this pathway represents an important inter...

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Main Authors: Dickerman, Benjamin K, McDonald, Jocelyn A, Sen, Ganes C
Format: Online
Language:English
Published: F1000Research 2014
Online Access:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3962003/
id pubmed-3962003
recordtype oai_dc
spelling pubmed-39620032014-04-07 The Human dsRNA binding protein PACT is unable to functionally substitute for the Drosophila dsRNA binding protein R2D2 Dickerman, Benjamin K McDonald, Jocelyn A Sen, Ganes C Research Article The dsRNA binding protein (dsRBP) PACT was first described as an activator of 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 in this pathway represents an important interplay between two modes of post-transcriptional gene regulation.  The function of PACT in this context is poorly understood.  Thus, additional approaches are required to clarify the mechanism by which PACT functions.  In this study, the genetic utility of  Drosophila melanogaster was employed to identify dsRNA-binding proteins that are functionally orthologous to PACT.  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. F1000Research 2014-03-28 /pmc/articles/PMC3962003/ /pubmed/24715958 http://dx.doi.org/10.12688/f1000research.2-220.v2 Text en Copyright: © 2014 Dickerman BK et al. http://creativecommons.org/licenses/by/3.0/ This is an open access article distributed under the terms of the Creative Commons Attribution Licence, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. http://creativecommons.org/publicdomain/zero/1.0/ Data associated with the article are available under the terms of the Creative Commons Zero "No rights reserved" data waiver (CC0 1.0 Public domain dedication).
repository_type Open Access Journal
institution_category Foreign Institution
institution US National Center for Biotechnology Information
building NCBI PubMed
collection Online Access
language English
format Online
author Dickerman, Benjamin K
McDonald, Jocelyn A
Sen, Ganes C
spellingShingle Dickerman, Benjamin K
McDonald, Jocelyn A
Sen, Ganes C
The Human dsRNA binding protein PACT is unable to functionally substitute for the Drosophila dsRNA binding protein R2D2
author_facet Dickerman, Benjamin K
McDonald, Jocelyn A
Sen, Ganes C
author_sort Dickerman, Benjamin K
title The Human dsRNA binding protein PACT is unable to functionally substitute for the Drosophila dsRNA binding protein R2D2
title_short The Human dsRNA binding protein PACT is unable to functionally substitute for the Drosophila dsRNA binding protein R2D2
title_full The Human dsRNA binding protein PACT is unable to functionally substitute for the Drosophila dsRNA binding protein R2D2
title_fullStr The Human dsRNA binding protein PACT is unable to functionally substitute for the Drosophila dsRNA binding protein R2D2
title_full_unstemmed The Human dsRNA binding protein PACT is unable to functionally substitute for the Drosophila dsRNA binding protein R2D2
title_sort human dsrna binding protein pact is unable to functionally substitute for the drosophila dsrna binding protein r2d2
description The dsRNA binding protein (dsRBP) PACT was first described as an activator of 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 in this pathway represents an important interplay between two modes of post-transcriptional gene regulation.  The function of PACT in this context is poorly understood.  Thus, additional approaches are required to clarify the mechanism by which PACT functions.  In this study, the genetic utility of  Drosophila melanogaster was employed to identify dsRNA-binding proteins that are functionally orthologous to PACT.  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.
publisher F1000Research
publishDate 2014
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3962003/
_version_ 1612070196202176512

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