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The MTR4 helicase recruits nuclear adaptors of the human RNA exosome using distinct arch-interacting motifs.
Nature 10:3393 (2019)
Publ. Version/Full Text
Research data
DOI
PMC
The nuclear exosome and its essential co-factor, the RNA helicase MTR4, play crucial roles in several RNA degradation pathways. Besides unwinding RNA substrates for exosome-mediated degradation, MTR4 associates with RNA-binding proteins that function as adaptors in different RNA processing and decay pathways. Here, we identify and characterize the interactions of human MTR4 with a ribosome processing adaptor, NVL, and with ZCCHC8, an adaptor involved in the decay of small nuclear RNAs. We show that the unstructured regions of NVL and ZCCHC8 contain short linear motifs that bind the MTR4 arch domain in a mutually exclusive manner. These short sequences diverged from the arch-interacting motif (AIM) of yeast rRNA processing factors. Our results suggest that nuclear exosome adaptors have evolved canonical and non-canonical AIM sequences to target human MTR4 and demonstrate the versatility and specificity with which the MTR4 arch domain can recruit a repertoire of different RNA-binding proteins.
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Publication type
Article: Journal article
Document type
Scientific Article
Keywords
Aaa-atpase Nvl2; Nmr-spectroscopy; Complex Reveals; Protein; Domain; Degradation; Multiple; Pathway; Mpp6; Rrp6
ISSN (print) / ISBN
0028-0836
e-ISSN
1476-4687
Journal
Nature
Quellenangaben
Volume: 10,
Issue: 1,
Article Number: 3393
Publisher
Nature Publishing Group
Publishing Place
London
Non-patent literature
Publications
Reviewing status
Peer reviewed
Institute(s)
Institute of Structural Biology (STB)