PMID:17289584

Citation	Luk, E, Vu, ND, Patteson, K, Mizuguchi, G, Wu, WH, Ranjan, A, Backus, J, Sen, S, Lewis, M, Bai, Y and Wu, C (2007) Chz1, a nuclear chaperone for histone H2AZ. Mol. Cell 25:357-68
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.
Links	PubMed Online version:10.1016/j.molcel.2006.12.015
Keywords	Adenosine Triphosphatases/metabolism; Amino Acid Sequence; Carrier Proteins/chemistry; Cell Cycle Proteins/physiology; Conserved Sequence; Dimerization; Histone Chaperones; Histones/metabolism; Humans; Molecular Chaperones/chemistry; Molecular Chaperones/metabolism; Molecular Chaperones/physiology; Molecular Sequence Data; Nuclear Proteins/physiology; Nucleosome Assembly Protein 1; Saccharomyces cerevisiae/genetics; Saccharomyces cerevisiae/metabolism; Saccharomyces cerevisiae Proteins/chemistry; Saccharomyces cerevisiae Proteins/metabolism; Saccharomyces cerevisiae Proteins/physiology; Sequence Alignment
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