Table 1.

Summary of the interactions among replisome components, histones and histone chaperones

Replisome proteins	Histone/histone chaperones	Methods used	Species
PCNA	CAF-1	IP: PCNA-CAF-1 physical interaction In vitro pull down: Cac1 (p150) subunit binds PCNA directly via the PIP domain	Homo sapiens, Saccharomyces cerevisiae
RFC	Asf1	In vitro pull down: Asf1 binds the Rfc1 subunit directly via the Asf1 N-terminal	Saccharomyces cerevisiae
	Rtt106	IP: Rtt106-Elg1-RFC physical interaction	Saccharomyces cerevisiae
RPA	FACT	In vitro pull down: Pob3-M domain binds RPA directly	Saccharomyces cerevisiae
	H3–H4/FACT, CAF-1, Rtt106	In vitro pull down: RPA binds H3-H4 directly. RPA binds FACT, CAF-1 and Rtt106 directly	Saccharomyces cerevisiae
Pol1 (Pol α)	H2A–H2B	IP: Yeast Pol1-(H2A–H2B) physical interaction In vitro pull down: N-terminal of human and yeast Pol1 has an H2A-H2B-binding domain	Saccharomyces cerevisiae, Homo sapiens
	FACT	IP: Pol α-FACT physical interaction In vitro pull down: Pol1 binds FACT directly	Saccharomyces cerevisiae
Dpb3-Dpb4 (Pol ε)	H2A–H2B	IP: Yeast Dpb3-Dpb4 has physical interaction with H2A-H2B and H3-H4	Saccharomyces cerevisiae, Schizosaccharomyces pombe
	H3–H4	Structural analysis and in vitro pull down: Dpb3-Dpb4 binds H3–H4 directly	Homo sapiens, Saccharomyces cerevisiae, Schizosaccharomyces pombe
Mcm2 (MCM2-7)	H3–H4	IP: Mcm2-(H3–H4) physical interaction In vitro pull down: N-terminal terminus of Mcm2 has a (H3–H4)-binding domain	Mus musculus, Homo sapiens, Saccharomyces cerevisiae
	Asf1	Structure analysis and in vitro pull down: H3–H4 dimer bridges the Asf1-Mcm2-7 interaction	Homo sapiens, Xenopus laevis
	FACT	In vitro pull down: FACT binds Mcm2 directly	Homo sapiens, Saccharomyces cerevisiae