The Argonaute-binding platform of NRPE1 evolves through modulation of intrinsically disordered repeats
AffiliationThe School of Plant Sciences, The University of Arizona
RNA-directed DNA methylation
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CitationThe Argonaute-binding platform of NRPE1 evolves through modulation of intrinsically disordered repeats 2016, 212 (4):1094 New Phytologist
Rights© 2016 The Authors. New Phytologist © 2016 New Phytologist Trust.
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Abstract• Argonaute proteins are important effectors in RNA silencing pathways, but they must interact with other machinery to trigger silencing. Ago hooks have emerged as a conserved motif responsible for interaction with Argonaute proteins, but little is know about the sequence surrounding Ago hooks that must restrict or enable interaction with specific Argonautes. • Here we investigated the evolutionary dynamics of an Argonaute-binding platform in NRPE1, the largest subunit of RNA Polymerase V. We compared NRPE1 sequences from more than 50 species, including dense sampling of two plant lineages. • This study demonstrates that the Argonaute-binding platform of NRPE1 retains Ago-hooks, intrinsic disorder, and repetitive character while being highly labile at the sequence level. We reveal that loss of sequence conservation is due to relaxed selection and frequent expansions and contractions of tandem repeat arrays. These factors allow a complete restructuring of the Ago-binding platform over 50-60 million years. This evolutionary pattern is also detected in a second Ago-binding platform, suggesting it is a general mechanism. • The presence of labile repeat arrays in all analyzed NRPE1 Ago-binding platforms indicates that selection maintains repetitive character, potentially to retain the ability to rapidly restructure the Ago-binding platform.
NoteVersion of record online: 19 July 2016; 12 month embargo.
VersionFinal accepted manuscript
SponsorsThis work is supported by National Science Foundation Grant MCB-1243608 to RAM.