Abstract
XRN2 is an essential eukaryotic exoribonuclease that processes and degrades various substrates. Here we identify the previously uncharacterized protein R05D11.6/PAXT-1 as a subunit of an XRN2 complex in C. elegans. Targeted paxt-1 inactivation through TALEN-mediated genome editing reduces XRN2 levels, decreases miRNA turnover activity, and results in worm death, which can be averted by overexpressing xrn-2. Hence, stabilization of XRN2 is a major function of PAXT-1. A truncated PAXT-1 protein retaining a predicted domain of unknown function (DUF3469) suffices to restore viability to paxt-1 mutant animals, elevates XRN2 levels, and binds to XRN2. This domain occurs in additional metazoan proteins and mediates interaction of human CDKN2AIP/CARF and NKRF/NRF with XRN2. Thus, we have identified a bona fide XRN2-binding domain (XTBD) that can link different proteins, and possibly functionalities, to XRN2.
Copyright © 2014 Elsevier Inc. All rights reserved.
Publication types
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Research Support, N.I.H., Extramural
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Research Support, Non-U.S. Gov't
MeSH terms
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Animals
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Apoptosis Regulatory Proteins / metabolism
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Binding Sites
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Caenorhabditis elegans / genetics
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Caenorhabditis elegans / metabolism*
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Caenorhabditis elegans Proteins / chemistry
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Caenorhabditis elegans Proteins / genetics
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Caenorhabditis elegans Proteins / metabolism*
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Carrier Proteins / chemistry
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Carrier Proteins / genetics
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Carrier Proteins / metabolism*
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Conserved Sequence
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DNA-Binding Proteins
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Exoribonucleases / metabolism
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Gene Knockout Techniques
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Humans
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Protein Structure, Tertiary
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RNA Stability
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RNA-Binding Proteins / metabolism
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Repressor Proteins / metabolism
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Transcription Factors / metabolism
Substances
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Apoptosis Regulatory Proteins
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CDKN2AIP protein, human
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CaRF protein, human
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Caenorhabditis elegans Proteins
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Carrier Proteins
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DNA-Binding Proteins
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NKRF protein, human
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PAXT-1 protein, C elegans
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RNA-Binding Proteins
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Repressor Proteins
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Transcription Factors
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Exoribonucleases
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XRN2 protein, human