期刊
MOLECULAR CELL
卷 53, 期 2, 页码 351-360出版社
CELL PRESS
DOI: 10.1016/j.molcel.2014.01.001
关键词
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资金
- European Union Seventh Framework Programme (FP7) [241985]
- Novartis Research Foundation through the FMI
- Swiss National Science Foundation [SNF 31003A_127052, SNF 31003A_143313]
- Boehringer Ingelheim Fonds PhD Fellowship
- NIH Office of Research Infrastructure Programs [P40 OD010440]
- Swiss National Science Foundation (SNF) [31003A_127052, 31003A_143313] Funding Source: Swiss National Science Foundation (SNF)
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 over-expressing 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.
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