RPA binds histone H3-H4 and functions in DNA replication-coupled nucleosome assembly

Shaofeng Liu, Zhiyun Xu, He Leng, Pu Zheng, Jiayi Yang, Kaifu Chen, Jianxun Feng, Qing Li

Research output: Contribution to journalArticle

28 Scopus citations

Abstract

DNA replication-coupled nucleosome assembly is essential to maintain genome integrity and retain epigenetic information. Multiple involved histone chaperones have been identified, but how nucleosome assembly is coupled to DNA replication remains elusive. Here we show that replication protein A (RPA), an essential replisome component that binds single-stranded DNA, has a role in replication-coupled nucleosome assembly. RPA directly binds free H3-H4. Assays using a synthetic sequence that mimics freshly unwound single-stranded DNA at replication fork showed that RPA promotes DNA-(H3-H4) complex formation immediately adjacent to double-stranded DNA. Further, an RPA mutant defective in H3-H4 binding exhibited attenuated nucleosome assembly on nascent chromatin. Thus, we propose that RPA functions as a platform for targeting histone deposition to replication fork, through which RPA couples nucleosome assembly with ongoing DNA replication.

Original languageEnglish (US)
Pages (from-to)415-420
Number of pages6
JournalScience
Volume355
Issue number6323
DOIs
StatePublished - 2021

ASJC Scopus subject areas

  • General

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