5fir
From Proteopedia
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== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/XRN2_CAEEL XRN2_CAEEL]] Possesses 5'->3' exoribonuclease activity. Plays a role in maintenance of steady-state concentration and turnover of microRNAs (miRNA) by degradation of mature miRNA. Partially redundant to xrn-1 in miRNA guide strand degradation. Implicated in differential regulation of mRNAs such as let-7 by controlling the accumulation of mature miRNA. Positively regulates molting of the pharyngeal cuticle.<ref>PMID:19734881</ref> <ref>PMID:21397849</ref> | [[http://www.uniprot.org/uniprot/XRN2_CAEEL XRN2_CAEEL]] Possesses 5'->3' exoribonuclease activity. Plays a role in maintenance of steady-state concentration and turnover of microRNAs (miRNA) by degradation of mature miRNA. Partially redundant to xrn-1 in miRNA guide strand degradation. Implicated in differential regulation of mRNAs such as let-7 by controlling the accumulation of mature miRNA. Positively regulates molting of the pharyngeal cuticle.<ref>PMID:19734881</ref> <ref>PMID:21397849</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The RNase XRN2 is essential in RNA metabolism. In Caenorhabditis elegans, XRN2 functions with PAXT-1, which shares a putative XRN2-binding domain (XTBD) with otherwise unrelated mammalian proteins. Here, we characterize the structure and function of an XTBD-XRN2 complex. Although XTBD stably interconnects two XRN2 domains through numerous interacting residues, mutation of a single critical residue suffices to disrupt XTBD-XRN2 complexes in vitro and to recapitulate paxt-1-null mutant phenotypes in vivo. Demonstrating conservation of function, vertebrate XTBD-containing proteins bind XRN2 in vitro, and human CDKN2AIPNL (HsC2AIL) can substitute for PAXT-1 in vivo. In vertebrates, which express three distinct XTBD-containing proteins, XRN2 may partition into distinct stable heterodimeric complexes, which probably differ in subcellular localization or function. In C. elegans, complex formation with PAXT-1, the sole XTBD protein, serves to preserve the stability of XRN2 in the absence of substrate. | ||
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| + | Structural basis and function of XRN2 binding by XTB domains.,Richter H, Katic I, Gut H, Grosshans H Nat Struct Mol Biol. 2016 Jan 18. doi: 10.1038/nsmb.3155. PMID:26779609<ref>PMID:26779609</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 5fir" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 18:42, 27 January 2016
Crystal structure of C. elegans XRN2 in complex with the XRN2-binding domain of PAXT-1
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