The Argonaute-binding platform of NRPE1 evolves through modulation of intrinsically disordered repeats.

ABSTRACT: Argonaute (Ago) 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 Ago proteins, but little is known about the sequence surrounding Ago hooks that must restrict or enable interaction with specific Argonautes. Here we investigated the evolutionary dynamics of an Ago-binding platform in NRPE1, the largest subunit of RNA polymerase V. We compared NRPE1 sequences from > 50 species, including dense sampling of two plant lineages. This study demonstrates that the Ago-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 conservatio

SUBMITTER: Trujillo JT 

PROVIDER: S-EPMC5125548 | biostudies-literature | 2016 Dec

REPOSITORIES: biostudies-literature