Characterization of the histone H2A.Z-1 and H2A.Z-2 isoforms in vertebrates

Dryhurst, Deanna; Ishibashi, Toyotaka; Rose, Kristie L.; Eirín‐López, José M.; McDonald, Darin; Silva-Moreno, Begonia; Veldhoen, Nik; Helbing, Caren C.; Hendzel, Michael J.; Shabanowitz, Jeffrey; Hunt, Donald F.; Ausió, Juan

doi:10.1186/1741-7007-7-86

Cited by 90 publications

(123 citation statements)

References 67 publications

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“…We generated two Flp-In TM -3T3 cell lines stably expressing either H2A or H2A.Z tagged with the SNAP epitope. Consistent with previous observations (Bulynko et al, 2006;Dryhurst et al, 2009;Greaves et al, 2007;Rangasamy et al, 2004), both variants showed a similar nuclear distribution and neither accumulated at the PHC at steady-state levels in our model system (supplementary material Fig. S1A,B).…”

Section: Different Dynamics Of H2a and H2az Deposition At Phcsupporting

confidence: 80%

Pericentric heterochromatin state during the cell cycle controls the histone variant composition of centromeres

Boyarchuk¹,

Filipescu²,

Vassias³

et al. 2014

Journal of Cell Science

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BSTRACTCorrect chromosome segregation requires a unique chromatin environment at centromeres and in their vicinity. Here, we address how the deposition of canonical H2A and H2A.Z histone variants is controlled at pericentric heterochromatin (PHC). Whereas in euchromatin newly synthesized H2A and H2A.Z are deposited throughout the cell cycle, we reveal two discrete waves of deposition at PHC -during mid to late S phase in a replicationdependent manner for H2A and during G1 phase for H2A.Z. This G1 cell cycle restriction is lost when heterochromatin features are altered, leading to the accumulation of H2A.Z at the domain. Interestingly, compromising PHC integrity also impacts upon neighboring centric chromatin, increasing the amount of centromeric CENP-A without changing the timing of its deposition. We conclude that the higher-order chromatin structure at the pericentric domain influences dynamics at the nucleosomal level within centromeric chromatin. The two different modes of rearrangement of the PHC during the cell cycle provide distinct opportunities to replenish one or the other H2A variant, highlighting PHC integrity as a potential signal to regulate the deposition timing and stoichiometry of histone variants at the centromere.

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Section: Different Dynamics Of H2a and H2az Deposition At Phcsupporting

confidence: 80%

Pericentric heterochromatin state during the cell cycle controls the histone variant composition of centromeres

Boyarchuk¹,

Filipescu²,

Vassias³

et al. 2014

Journal of Cell Science

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“…The lack of any phenotypic effects when H2A.Z expression is knocked down in these cells could indicate that the residual amounts of H2A.Z are sufficient to sustain growth and differentiation of C2C12 cells. In addition, recent studies showed that there are in fact two isoforms of H2A.Z encoded by distinct genes (49,50). Because our shRNA specifically targets H2A.Z-1 but not the H2A.Z-2 isoform, it is a formal possibility that the H2A.Z-2 isoform in these cells is sufficient to compensate for the loss of H2A.Z-1 in these cells.…”

Section: Discussionmentioning

confidence: 94%

Expression of Non-acetylatable H2A.Z in Myoblast Cells Blocks Myoblast Differentiation through Disruption of MyoD Expression

Law

Cheung

2015

Journal of Biological Chemistry

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Background: H2A.Z is a histone variant that replaces H2A at strategic locations within the genome. Results: Expression of non-acetylatable H2A.Z blocks myogenic differentiation. Conclusion: H2A.Z acetylation is important for MyoD expression in myoblasts, which in turn is required for myogenesis.Significance: These results demonstrate that expression of a mutant H2A.Z can lead to dysregulation and inhibition of cellular differentiation programs.

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“…Z.2), another monophyletic lineage within H2A. 39,50,51 In both cases, the differentiation of specialized vertebrate variants is concomitant with an increase in organismal complexity, underscoring the role of these variants in refining chromatin structure and the associated epigenetic mechanisms. On the contrary, the apparent absence of macroH2A in some protostome groups (i.e., nematodes and holometabolous insects) indicates that this variant might not be indispensable for the correct development of all organisms.…”

Section: Discussionmentioning

confidence: 99%

The characterization of macroH2A beyond vertebrates supports an ancestral origin and conserved role for histone variants in chromatin

et al. 2016

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Histone variants play a critical role in chromatin structure and epigenetic regulation. These "deviant" proteins have been historically considered as the evolutionary descendants of ancestral canonical histones, helping specialize the nucleosome structure during eukaryotic evolution. Such view is now challenged by 2 major observations: first, canonical histones present extremely unique features not shared with any other genes; second, histone variants are widespread across many eukaryotic groups. The present work further supports the ancestral nature of histone variants by providing the first in vivo characterization of a functional macroH2A histone (a variant long defined as a specific refinement of vertebrate chromatin) in a non-vertebrate organism (the mussel Mytilus) revealing its recruitment into heterochromatic fractions of actively proliferating tissues. Combined with in silico analyses of genomic data, these results provide evidence for the widespread presence of macroH2A in metazoan animals, as well as in the holozoan Capsaspora, supporting an evolutionary origin for this histone variant lineage before the radiation of Filozoans (including Filasterea, Choanoflagellata and Metazoa). Overall, the results presented in this work help configure a new evolutionary scenario in which histone variants, rather than modern "deviants" of canonical histones, would constitute ancient components of eukaryotic chromatin.

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Characterization of the histone H2A.Z-1 and H2A.Z-2 isoforms in vertebrates

Cited by 90 publications

References 67 publications

Pericentric heterochromatin state during the cell cycle controls the histone variant composition of centromeres

Pericentric heterochromatin state during the cell cycle controls the histone variant composition of centromeres

Expression of Non-acetylatable H2A.Z in Myoblast Cells Blocks Myoblast Differentiation through Disruption of MyoD Expression

The characterization of macroH2A beyond vertebrates supports an ancestral origin and conserved role for histone variants in chromatin

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