4.7 Article

Structural Basis for the Unique Multivalent Readout of Unmodified H3 Tail by Arabidopsis ORC1b BAH-PHD Cassette

期刊

STRUCTURE
卷 24, 期 3, 页码 486-494

出版社

CELL PRESS
DOI: 10.1016/j.str.2016.01.004

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资金

  1. Thousand Young Talent Program of China
  2. Chinese Academy of Sciences
  3. LLSCOR Program Project
  4. STARR Foundation
  5. NIH [GM060398, GM079641]
  6. Memorial Sloan-Kettering Cancer Center Support Grant/Core Grant [P30 CA008748]

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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.

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