Chaston, Jessica J and Stewart, Alastair G and Christie, Mary (2017) Structural characterisation of TNRC6A nuclear localisation signal in complex with importin-alpha. PloS One, 12 (8). pp. e0183587. ISSN 1932-6203 (Gold OA)
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Abstract
The GW182/TNRC6 family of proteins are central scaffolds that link microRNA-associated Argonaute proteins to the cytoplasmic decay machinery for targeted mRNA degradation processes. Although nuclear roles for the GW182/TNRC6 proteins are unknown, recent reports have demonstrated nucleocytoplasmic shuttling activity that utilises the importin-α and importin-β transport receptors for nuclear translocation. Here we describe the structure of mouse importin-α in complex with the TNRC6A nuclear localisation signal peptide. We further show that the interactions observed between TNRC6A and importin-α are conserved between mouse and human complexes. Our results highlight the ability of monopartite cNLS sequences to maximise contacts at the importin-α major binding site, as well as regions outside the main binding cavities.
Item Type: | Article |
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Subjects: | R Medicine > R Medicine (General) |
Depositing User: | Repository Administrator |
Date Deposited: | 28 Aug 2017 01:30 |
Last Modified: | 30 Jan 2018 05:40 |
URI: | https://eprints.victorchang.edu.au/id/eprint/623 |
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