The Cac2 subunit is essential for productive histone binding and nucleosome assembly in CAF-1

被引:21
作者
Mattiroli, Francesca [1 ,2 ]
Gu, Yajie [2 ,3 ]
Balsbaugh, Jeremy L. [2 ]
Ahn, Natalie G. [4 ]
Luger, Karolin [1 ,2 ,5 ]
机构
[1] Univ Colorado Boulder, Howard Hughes Med Inst, Dept Chem & Biochem, Boulder, CO 80303 USA
[2] Univ Colorado, Dept Chem & Biochem, Boulder, CO 80303 USA
[3] Colorado State Univ, Dept Biochem & Mol Biol, Ft Collins, CO 80523 USA
[4] Univ Colorado, Biofrontiers Inst, Dept Chem & Biochem, Boulder, CO 80303 USA
[5] Colorado State Univ, Inst Genome Architecture & Funct, Ft Collins, CO 80523 USA
基金
美国国家卫生研究院;
关键词
FACTOR-I; CHROMATIN REPLICATION; HYDROGEN-EXCHANGE; DNA-REPLICATION; PCNA; ASF1; COMPLEX; INHERITANCE; CHAPERONES; REPAIR;
D O I
10.1038/srep46274
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
Nucleosome assembly following DNA replication controls epigenome maintenance and genome integrity. Chromatin assembly factor 1 (CAF-1) is the histone chaperone responsible for histone (H3-H4)(2) deposition following DNA synthesis. Structural and functional details for this chaperone complex and its interaction with histones are slowly emerging. Using hydrogen-deuterium exchange coupled to mass spectrometry, combined with in vitro and in vivo mutagenesis studies, we identified the regions involved in the direct interaction between the yeast CAF-1 subunits, and mapped the CAF-1 domains responsible for H3-H4 binding. The large subunit, Cac1 organizes the assembly of CAF-1. Strikingly, H3-H4 binding is mediated by a composite interface, shaped by Cac1-bound Cac2 and the Cac1 acidic region. Cac2 is indispensable for productive histone binding, while deletion of Cac3 has only moderate effects on H3-H4 binding and nucleosome assembly. These results define direct structural roles for yeast CAF-1 subunits and uncover a previously unknown critical function of the middle subunit in CAF-1.
引用
收藏
页数:11
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