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Genes to Cells (2008) 13, 1027-1043. doi:10.1111/j.1365-2443.2008.01225.x
© 2008 Blackwell Publishing or its licensors

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Fission yeast chromatin assembly factor 1 assists in the replication-coupled maintenance of heterochromatin

Kohei Dohke1,2,a, Shota Miyazaki1,2,b, Katsunori Tanaka3, Takeshi Urano4, Shiv I. S. Grewal5 and Yota Murakami1,*

1 Department of Cell Biology, Institute for Virus Research, and
2 Department of Mammalian Regulatory Network, Graduate School of Biostudies, Kyoto University, Sakyo-ku, Kyoto 606-8507, Japan
3 Department of Bioscience, School of Science and Technology, Kwansei Gakuin University, Sanda, Hyogo 669-1337, Japan
4 Laboratory of Biochemistry II, School of Medicine, Shimane University, Izumo, Shimane 693-8501, Japan
5 Laboratory of Biochemistry and Molecular Biology, National Cancer Institute, National Institutes of Health, Bethesda, MA 20892, USA

Chromatin assembly factor-1 (CAF1) is a well-conserved histone chaperone that loads the histone H3-H4 complex onto newly synthesized DNA in vitro through interaction with the replication factor PCNA. CAF1 is considered to be involved in heterochromatin maintenance in several organisms, but the evidence is circumstantial and functional details have not been established. We identified fission yeast CAF-1 (spCAF1), which interacts with PCNA in S phase. Depletion of spCAF1 caused defects in silencing at centromeric and mating locus heterochromatin, accompanied with a decrease in Swi6, the fission yeast HP1 homologue. Loss of spCAF1 destabilized both the silent and active states of chromatin at the meta-stable heterochromatic region, with a more pronounced effect on the silent state, indicating that spCAF1 is involved in the maintenance of heterochromatin. Swi6 dissociated from heterochromatin during G1/S phase appears to associate with spCAF1. In early S phase, spCAF1 localized to replicating heterochromatin as well as euchromatin and remained associated with Swi6, and Swi6 then bound to heterochromatin. Taken together, we propose that spCAF1 functions in heterochromatin maintenance by recruiting dislocated Swi6 during replication to replicated heterochromatin at the replication fork.


Communicated by: Fuyuki Ishikawa

aPresent address: Graduate School of Natural Sciences, Nagoya City University, Mizuho-ku, Nagoya 467-8601, Japan.

bPresent address: GL Sciences Inc., 237-2 Sayamagahara, Iruma, Saitama 358-0032, Japan.

* Correspondence: yota{at}virus.kyoto-u.ac.jp







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