| Literature DB >> 26876097 |
Sisi Li1, Zhenlin Yang2, Xuan Du2, Rui Liu3, Alex W Wilkinson4, Or Gozani4, Steven E Jacobsen5, Dinshaw J Patel1, Jiamu Du6.
Abstract
DNA replication initiation relies on the formation of the origin recognition complex (ORC). The plant ORC subunit 1 (ORC1) protein possesses a conserved N-terminal BAH domain with an embedded plant-specific PHD finger, whose function may be potentially regulated by an epigenetic mechanism. Here, we report structural and biochemical studies on the Arabidopsis thaliana ORC1b BAH-PHD cassette which specifically recognizes the unmodified H3 tail. The crystal structure of ORC1b BAH-PHD cassette in complex with an H3(1-15) peptide reveals a strict requirement for the unmodified state of R2, T3, and K4 on the H3 tail and a novel multivalent BAH and PHD readout mode for H3 peptide recognition. Such recognition may contribute to epigenetic regulation of the initiation of DNA replication.Entities:
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Year: 2016 PMID： 26876097 PMCID： PMC4775424 DOI： 10.1016/j.str.2016.01.004
Source DB: PubMed Journal: Structure ISSN： 0969-2126 Impact factor: 5.006