Schultz et al. (1998) Proc. Natl. Acad. Sci. USA 95, 5857-5864
Letunic et al. (2012) Nucleic Acids Res , doi:10.1093/nar/gkr931

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CHZ Histone chaperone domain CHZ

SMART accession number:	SM01082
Description:	This domain is highly conserved from yeasts to humans and is part of the chaperone protein HIRIP3 in vertebrates which interacts with the H3.3 chaperone HIRA, implicated in histone replacement during transcription. N- and C- termini of Chz family members are relatively divergent but do contain similar acidic stretches rich in Glu/Asp residues, characteristic of all histone chaperones (PUBMED:17289584).
Interpro abstract (IPR019098):	This domain is highly conserved from yeasts to humans and is part of the chaperone protein HIRIP3 in vertebrates which interacts with the H3.3 chaperone HIRA, implicated in histone replacement during transcription. N- and C- termini of Chz family members are relatively divergent but do contain similar acidic stretches rich in Glu/Asp residues, characteristic of all histone chaperones [(PUBMED:17289584)].
Family alignment:	View or CHROMA formatCLUSTALW formatMSF formatFASTA formatPIR format

There are 100 CHZ domains in 100 proteins in SMART's nrdb database.

Click on the following links for more information.

• Evolution (species in which this domain is found)

• Click on to expand nodes. To display all proteins with a CHZ domain in a specific node, click on it.

  This tree shows only several representative species. The complete taxonomic breakdown of all proteins with CHZ domain is also avaliable.

  Useful shortcuts: Expand all nodes or Collapse tree
  Go to specific node: Arabidopsis thaliana, Homo sapiens, Mus musculus, Rattus norvegicus, Saccharomyces cerevisiae

• Cellular role (predicted cellular role)

• Cellular role: interaction
  

• Literature (relevant references for this domain)

• Primary literature is listed below; Automatically-derived, secondary literature is also avaliable.

  • Luk E et al.
  • Chz1, a nuclear chaperone for histone H2AZ.
  • Mol Cell. 2007; 25: 357-68
  • Display abstract

  • The histone variant H2AZ marks nucleosomes flanking the promoters of mostgenes of budding yeast. The incorporation of H2AZ into chromatin isdependent on the SWR1 complex, which catalyses the replacement ofconventional histone H2A with H2AZ. In cells, the pool of unincorporatedhistone H2AZ has previously been found in association with Nap1, achaperone for conventional histone H2A-H2B. Here, we report the discoveryof Chz1, a histone chaperone that has preference for H2AZ and can alsodeliver a source of the histone variant for SWR1-dependent histonereplacement. Bacterially expressed Chz1 forms a heterotrimer withH2AZ-H2B, stabilizing the association of the histone dimer. We haveidentified a conserved motif important for histone variant recognitionwithin the H2AZ-interacting domain of Chz1. The presence of this motif inother metazoan proteins suggests that H2AZ-specific chaperones may bewidely conserved.

• Structure (3D structures containing this domain)

• 3D Structures of CHZ domains in PDB

  PDB code	Main view	Title
  2jss		Nmr structure of chaperone chz1 complexed with histone h2a.z-h2b

• Links (links to other resources describing this domain)

• PFAM	CHZ
  INTERPRO	IPR019098

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