Structural basis for the unique multivalent readout of unmodified H3 tail by Arabidopsis ORC1b BAH-PHD cassette Journal Article

   

Authors:	Li, S.; Yang, Z.; Du, X.; Liu, R.; Wilkinson, A. W.; Gozani, O.; Jacobsen, S. E.; Patel, D. J.; Du, J.
Article Title:	Structural basis for the unique multivalent readout of unmodified H3 tail by Arabidopsis ORC1b BAH-PHD cassette
Abstract:	Summary 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. © 2016 Elsevier Ltd. All rights reserved.
Journal Title:	Structure
Volume:	24
Issue:	3
ISSN:	0969-2126
Publisher:	Cell Press
Date Published:	2016-03-01
Start Page:	486
End Page:	494
Language:	English
DOI:	10.1016/j.str.2016.01.004
PROVIDER:	scopus
PMCID:	PMC4775424
PUBMED:	26876097
DOI/URL:	http://www.scopus.com/inward/record.url?eid=2-s2.0-84959345759&partnerID=40&md5=2d20c42352c726d14e10d9c63ba76b55
Notes:	Article -- Export Date: 4 April 2016 -- Source: Scopus

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