The BioGRID | PUBLICATION VIEW

	Mol. Cell Feb (2007); 25(3):357-68
Chz1, a nuclear chaperone for histone H2AZ-
Luk E, Vu ND, Patteson K, Mizuguchi G, Wu WH, Ranjan A, Backus J, Sen S, Lewis M, Bai Y, Wu C
Laboratory of Biochemistry and Molecular Biology, National Cancer Institute, National Institutes of Health, Bethesda, MD 20892, USA- luked@mail-nih-gov
Abstract: The histone variant H2AZ marks nucleosomes flanking the promoters of most genes of budding yeast- The incorporation of H2AZ into chromatin is dependent on the SWR1 complex, which catalyses the replacement of conventional histone H2A with H2AZ- In cells, the pool of unincorporated histone H2AZ has previously been found in association with Nap1, a chaperone for conventional histone H2A-H2B- Here, we report the discovery of Chz1, a histone chaperone that has preference for H2AZ and can also deliver a source of the histone variant for SWR1-dependent histone replacement- Bacterially expressed Chz1 forms a heterotrimer with H2AZ-H2B, stabilizing the association of the histone dimer- We have identified a conserved motif important for histone variant recognition within the H2AZ-interacting domain of Chz1- The presence of this motif in other metazoan proteins suggests that H2AZ-specific chaperones may be widely conserved-
[PUBMED: 17289584]