Abstract:
:Chromatin assembly factor 1 (CAF-1) is a histone H3-H4 chaperone that deposits newly synthesized histone (H3-H4)2 tetramers during replication-coupled nucleosome assembly. However, how CAF-1 functions in this process is not yet well understood. Here, we report the crystal structure of C terminus of Cac1 (Cac1C), a subunit of yeast CAF-1, and the function of this domain in stabilizing CAF-1 at replication forks. We show that Cac1C forms a winged helix domain (WHD) and binds DNA in a sequence-independent manner. Mutations in Cac1C that abolish DNA binding result in defects in transcriptional silencing and increased sensitivity to DNA damaging agents, and these defects are exacerbated when combined with Cac1 mutations deficient in PCNA binding. Similar phenotypes are observed for corresponding mutations in mouse CAF-1. These results reveal a mechanism conserved in eukaryotic cells whereby the ability of CAF-1 to bind DNA is important for its association with the DNA replication forks and subsequent nucleosome assembly.
journal_name
Nucleic Acids Resjournal_title
Nucleic acids researchauthors
Zhang K,Gao Y,Li J,Burgess R,Han J,Liang H,Zhang Z,Liu Ydoi
10.1093/nar/gkw106subject
Has Abstractpub_date
2016-06-20 00:00:00pages
5083-94issue
11eissn
0305-1048issn
1362-4962pii
gkw106journal_volume
44pub_type
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