Structural Basis and Function of XRN2-Binding by XTB Domains

Structural Basis and Function of XRN2-Binding by XTB Domains

The ribonuclease XRN2 is an essential player 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 structure and function of an XTBD – XRN2 complex. Although XTBD...

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Main Authors: Richter, Hannes, Katic, Iskra, Gut, Heinz, Großhans, Helge
Format: Online
Language:English
Published: 2016
Online Access:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4888950/
id pubmed-4888950
recordtype oai_dc
spelling pubmed-48889502016-08-01 Structural Basis and Function of XRN2-Binding by XTB Domains Richter, Hannes Katic, Iskra Gut, Heinz Großhans, Helge Article The ribonuclease XRN2 is an essential player 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 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 recapitulates paxt-1 null mutant phenotypes in vivo. Demonstrating conservation of function, vertebrate XTBD-containing proteins bind XRN2 in vitro, and human CDKN2AIPNL (C2AIL) can substitute for PAXT-1 in vivo. In vertebrates, where three distinct XTBD-containing proteins exist, XRN2 may partition to distinct stable heterodimeric complexes, likely differing in subcellular localization or function. In C. elegans, complex formation with the unique PAXT-1 serves to preserve the stability of XRN2 in the absence of substrate. 2016-01-18 2016-02 /pmc/articles/PMC4888950/ /pubmed/26779609 http://dx.doi.org/10.1038/nsmb.3155 Text en Users may view, print, copy, and download text and data-mine the content in such documents, for the purposes of academic research, subject always to the full Conditions of use:http://www.nature.com/authors/editorial_policies/license.html#terms
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 Richter, Hannes
Katic, Iskra
Gut, Heinz
Großhans, Helge
spellingShingle Richter, Hannes
Katic, Iskra
Gut, Heinz
Großhans, Helge
Structural Basis and Function of XRN2-Binding by XTB Domains
author_facet Richter, Hannes
Katic, Iskra
Gut, Heinz
Großhans, Helge
author_sort Richter, Hannes
title Structural Basis and Function of XRN2-Binding by XTB Domains
title_short Structural Basis and Function of XRN2-Binding by XTB Domains
title_full Structural Basis and Function of XRN2-Binding by XTB Domains
title_fullStr Structural Basis and Function of XRN2-Binding by XTB Domains
title_full_unstemmed Structural Basis and Function of XRN2-Binding by XTB Domains
title_sort structural basis and function of xrn2-binding by xtb domains
description The ribonuclease XRN2 is an essential player 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 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 recapitulates paxt-1 null mutant phenotypes in vivo. Demonstrating conservation of function, vertebrate XTBD-containing proteins bind XRN2 in vitro, and human CDKN2AIPNL (C2AIL) can substitute for PAXT-1 in vivo. In vertebrates, where three distinct XTBD-containing proteins exist, XRN2 may partition to distinct stable heterodimeric complexes, likely differing in subcellular localization or function. In C. elegans, complex formation with the unique PAXT-1 serves to preserve the stability of XRN2 in the absence of substrate.
publishDate 2016
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4888950/
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