A Protein Complex Containing the Conserved Swi2/Snf2-Related ATPase Swr1p Deposits Histone Variant H2A.Z into Euchromatin

By Michael S. Kobor, S. Venkatasubrahmanyam, M. Meneghini, J. Gin, Jennifer L. Jennings, A. Link, H. Madhani, J. Rine. PLoS Biology, 2004

682 citations recorded by the source corpus.

The conserved histone variant H2A.Z functions in euchromatin to antagonize the spread of heterochromatin. The mechanism by which histone H2A is replaced by H2A.Z in the nucleosome is unknown. We identified a complex containing 13 different polypeptides associated with a soluble pool of H2A.Z in Saccharomyces cerevisiae. This complex was designated SWR1-Com in reference to the Swr1p subunit, a Swi2/Snf2-paralog. Swr1p and six other subunits were found only in SWR1-Com, whereas six other subunits were also found in the NuA4 histone acetyltransferase and/or the Ino80 chromatin remodeling complex. H2A.Z and SWR1 were essential for viability of cells lacking the EAF1 component of NuA4, pointing to a close functional connection between these two complexes. Strikingly, chromatin immunoprecipitation analysis of cells lacking Swr1p, the presumed ATPase of the complex, revealed a profound defect in the deposition of H2A.Z at euchromatic regions that flank the silent mating type cassette HMR and at 12 other chromosomal sites tested. Consistent with a specialized role for Swr1p in H2A.Z deposition, the majority of the genome-wide transcriptional defects seen in swr1Δ cells were also found in htz1Δ cells. These studies revealed a novel role for a member of the ATP-dependent chromatin remodeling enzyme family in determining the region-specific histone subunit composition of chromatin in vivo and controlling the epigenetic state of chromatin. Metazoan orthologs of Swr1p (Drosophila Domino; human SRCAP and p400) may have analogous functions.

Subfields: Molecular Biology

View Paper: https://www.semanticscholar.org/paper/8ef68193ef6df6ec6199b715574d761fef9c4177

How researchers see this paper

The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.

In Molecular Biology

Citations in the corpus

Histone variant H2A.Z marks the 5' ends of both active and inactive genes in euchromatin. (2005, background): “Z in vivo (Kobor et al., 2004; Krogan et al., 2003b; Mizuguchi et al., 2004).”
Navigating the chaperone network: an integrative map of physical and genetic interactions mediated by the hsp90 chaperone. (2005, background): “…subunits of a recently discovered 13 R protein chromatin remodeling complex, SWR-C, which regulates gene transcription near silent heterochroma- t atin by facilitating recruitment of the histone H2A variant, Htz1, into chromatin (Krogan et al., 2003; Mizuguchi et S tal., 2004; Kobor et al., 2004).”
Cotranscriptional set2 methylation of histone H3 lysine 36 recruits a repressive Rpd3 complex. (2005, neutral): “Z into chromatin (Kobor et al., 2004; Krogan et al., 2003b; Mizuguchi et al., 2004).”
The X and Y Chromosomes Assemble into H2A.Z, Containing Facultative Heterochromatin, following Meiosis (2006, background): “chromatin loci (31, 32, 42), is required for telomeric silencing”
Dynamic regulation of nucleosome positioning in the human genome. (2008, positive): “Z by the ATP-dependent Ino80 into nucleosomes (Kobor et al., 2004; Krogan et al., 2003; Mizuguchi et al., 2004) may also facilitate nucleosome eviction or repositioning by destabilizing the nucleosome structure (Luger et al.”
H2A.Z-containing nucleosomes mediate the thermosensory response in Arabidopsis. (2010, neutral): “Z into nucleosomes in place of H2A (Deal et al., 2007; Kobor et al., 2004; Krogan et al., 2003; Mizuguchi et al., 2004).”
Toward a Comprehensive Atlas of the Physical Interactome of Saccharomyces cerevisiae*S (2007, background): “Visual inspection of the off-diagonal connections demonstrates that the DNA helicases Rvb1 and Rvb2 are components of the INO80C, SWR-C, and Tah1-Pih1, but not NuA4, protein complexes (Fig.”