An acetylated form of histone H2A.Z regulates chromosome architecture in Schizosaccharomyces pombe

Kim, Hyun Soo; Vanoosthuyse, Vincent; Fillingham, Jeffrey; Roguev, Assen; Watt, Stephen; Kislinger, Thomas; Treyer, Alex; Carpenter, Laura Rocco; Bennett, Christopher S; Emili, Andrew; Greenblatt, Jack; Hardwick, Kevin; Krogan, Nevan J.; Bähler, Jürg; Keogh, Michael‐Christopher

doi:10.1038/nsmb.1688

Cited by 80 publications

(121 citation statements)

References 57 publications

(83 reference statements)

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“…In addition, phenotypes of cells deleted for msc1 are similar to those of cells deleted for pht1, the gene encoding histone H2A.Z in Schizosaccharomyces pombe (2). Studies from multiple groups demonstrate that the Msc1 protein is a component of the Swr1 chromatin-remodeling complex (3)(4)(5)(6), confirming genetic and proteomic predictions (7,8). Swr1 complexes from a variety of organisms facilitate the incorporation of the histone variant H2A.Z into chromatin in exchange for histone H2A (9,10).…”

supporting

confidence: 48%

Activity of a C-terminal Plant Homeodomain (PHD) of Msc1 Is Essential for Function

Qiu¹,

Dul

Walworth

2010

Journal of Biological Chemistry

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Msc1, a member of the Jarid1 family of putative histone demethylases, is required for chromosome stability in fission yeast. Msc1 associates with the Swr1 complex that facilitates deposition of histone H2A.Z into chromatin. To assess the function of Msc1 in the Swr1 complex, domains of Msc1 necessary for interaction with Swr1 were identified. The C-terminal plant homeodomain (PHD) 2 and PHD3 of Msc1 are sufficient to confer association with Swr1 and allow Msc1 to function in the context of kinetochore mutants. On the other hand, a mutant with a single amino acid substitution in PHD2 within the full-length Msc1 protein retains the ability to bind to Swr1 but eliminates the function of Msc1 in combination with kinetochore mutants. Thus, Swr1 association is critical but not sufficient for Msc1 function. An activity of Msc1 that depends on the cysteine residue within PHD2 of Msc1 is likewise critical for function. On the basis of our observation that the PHDs of Msc1 act as E3 ubiquitin ligases and that mutations of cysteine residues within those domains abolish ligase activity, we speculate that the ability of Msc1 to facilitate ubiquitin transfer is critical for the function it mediates through its association with Swr1.

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supporting

confidence: 48%

Activity of a C-terminal Plant Homeodomain (PHD) of Msc1 Is Essential for Function

Qiu¹,

Dul

Walworth

2010

Journal of Biological Chemistry

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“…In Schizosaccharomyces pombe, an acetylated form of H2A.Z regulates chromosome architecture. 32 In Saccharomyces cerevisae, the sumoylation of H2A.Z is important for chromosome fixation to the nuclear periphery after a persistent DNA double-stranded-break. 33 For more details on H2A.Z post-translational modifications, see refs.…”

Section: H2az and Dna Methylationmentioning

confidence: 99%

Reconciling the positive and negative roles of histone H2A.Z in gene transcription

Marques

Laflamme²,

Gervais³

et al. 2010

Epigenetics

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“…The H2A.Z histone variant is enriched in the centromeres and pericentric heterochromatin of mammals and is an important component of the three-dimensional structure of the mouse centromere (Greaves et al 2007). H2A.Z enrichment has also been found in the pericentric heterochromatin of fission yeast, suggesting that this may be a conserved constituent of regional centromeres (Kim et al 2009). In both mammals and fission yeast, H2A.Z depletion leads to chromosome segregation defects (Carr et al 1994;Rangasamy et al 2003;Greaves et al 2007;Hou et al 2010), suggesting that H2A.Z contributes to proper centromere-kinetochore attachments during mitosis (Boyarchuk et al 2011).…”

mentioning

confidence: 99%

The INO80 chromatin remodeling complex prevents polyploidy and maintains normal chromatin structure at centromeres

et al. 2012

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The INO80 chromatin remodeling complex functions in transcriptional regulation, DNA repair, and replication. Here we uncover a novel role for INO80 in regulating chromosome segregation. First, we show that the conserved Ies6 subunit is critical for INO80 function in vivo. Strikingly, we found that loss of either Ies6 or the Ino80 catalytic subunit results in rapid increase in ploidy. One route to polyploidy is through chromosome missegregation due to aberrant centromere structure, and we found that loss of either Ies6 or Ino80 leads to defective chromosome segregation. Importantly, we show that chromatin structure flanking centromeres is altered in cells lacking these subunits and that these alterations occur not in the Cse4-containing centromeric nucleosome, but in pericentric chromatin. We provide evidence that these effects are mediated through misincorporation of H2A.Z, and these findings indicate that H2A.Z-containing pericentric chromatin, as in higher eukaryotes with regional centromeres, is important for centromere function in budding yeast. These data reveal an important additional mechanism by which INO80 maintains genome stability.

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An acetylated form of histone H2A.Z regulates chromosome architecture in Schizosaccharomyces pombe

Cited by 80 publications

References 57 publications

Activity of a C-terminal Plant Homeodomain (PHD) of Msc1 Is Essential for Function

Activity of a C-terminal Plant Homeodomain (PHD) of Msc1 Is Essential for Function

Reconciling the positive and negative roles of histone H2A.Z in gene transcription

The INO80 chromatin remodeling complex prevents polyploidy and maintains normal chromatin structure at centromeres

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