DNA unwinding at eukaryotic replication forks displaces parental histones, which 
must be redeposited onto nascent DNA in order to preserve chromatin structure. 
By screening systematically for replisome components that pick up histones 
released from chromatin into a yeast cell extract, we found that the Mcm2 
helicase subunit binds histones cooperatively with the FACT (facilitiates 
chromatin transcription) complex, which helps to re-establish chromatin during 
transcription. FACT does not associate with the Mcm2-7 helicase at replication 
origins during G1 phase but is subsequently incorporated into the replisome 
progression complex independently of histone binding and uniquely among histone 
chaperones. The amino terminal tail of Mcm2 binds histones via a conserved motif 
that is dispensable for DNA synthesis per se but helps preserve subtelomeric 
chromatin, retain the 2 micron minichromosome, and support growth in the absence 
of Ctf18-RFC. Our data indicate that the eukaryotic replication and 
transcription machineries use analogous assemblies of multiple chaperones to 
preserve chromatin integrity.