Histone H2A variants H2AX and H2AZ (Q28207014)

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Duane Pilch

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Emmy Rogakou

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Olga Sedelnikova

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Kenneth Newrock

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William Bonner

Current Opinion in Genetics & Development

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publication date

April 2002

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language of work or name

English

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published in

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volume

12

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issue

2

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page(s)

162-9

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publication type of scholarly work

review article

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Non-allelic variants of histones 2a, 2b and 3 in mammals

Europe PubMed Central

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Histone 2A, a heteromorphous family of eight protein species

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MacroH2A, a core histone containing a large nonhistone region

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MACROH2A2, a new member of the MARCOH2A core histone family

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Histone H2A variants and the inactive X chromosome: identification of a second macroH2A variant

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A novel chromatin protein, distantly related to histone H2A, is largely excluded from the inactive X chromosome

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H2A.X. a histone isoprotein with a conserved C-terminal sequence, is encoded by a novel mRNA with both DNA replication type and polyA 3' processing signals

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Histone H2A.Z has a conserved function that is distinct from that of the major H2A sequence variants

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Essential and nonessential histone H2A variants in Tetrahymena thermophila

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DNA Double-stranded Breaks Induce Histone H2AX Phosphorylation on Serine 139

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Megabase chromatin domains involved in DNA double-strand breaks in vivo

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A critical role for histone H2AX in recruitment of repair factors to nuclear foci after DNA damage

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ATM phosphorylates histone H2AX in response to DNA double-strand breaks

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p53 binding protein 1 (53BP1) is an early participant in the cellular response to DNA double-strand breaks

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Tumor suppressor p53 binding protein 1 (53BP1) is involved in DNA damage-signaling pathways

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Histone H2AX Is Phosphorylated in an ATR-dependent Manner in Response to Replicational Stress

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A role for Saccharomyces cerevisiae histone H2A in DNA repair.

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Response to RAG-mediated VDJ cleavage by NBS1 and gamma-H2AX

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Recombinational DNA double-strand breaks in mice precede synapsis

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Initiation of DNA fragmentation during apoptosis induces phosphorylation of H2AX histone at serine 139

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Two complexes that contain histones are required for nucleosome assembly in vitro: role of nucleoplasmin and N1 in Xenopus egg extracts

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DNA-dependent phosphorylation of histone H2A.X during nucleosome assembly in Xenopus laevis oocytes: involvement of protein phosphorylation in nucleosome spacing.

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Mre11 protein complex prevents double-strand break accumulation during chromosomal DNA replication.

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Minor Histone 2A Variants and Ubiquinated Forms in the Native H2A:H2B Dimer

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H2A.F: an extremely variant histone H2A sequence expressed in the chicken embryo

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Sequence of cDNAs for mammalian H2A.Z, an evolutionarily diverged but highly conserved basal histone H2A isoprotein species

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Either of the major H2A genes but not an evolutionarily conserved H2A.F/Z variant of Tetrahymena thermophila can function as the sole H2A gene in the yeast Saccharomyces cerevisiae

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Histone H2A.Z regulats transcription and is partially redundant with nucleosome remodeling complexes

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Analysis of a histone H2A variant from fission yeast: evidence for a role in chromosome stability.

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Regions of variant histone His2AvD required for Drosophila development

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A histone variant, H2AvD, is essential in Drosophila melanogaster

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Histone variant H2A.Z is required for early mammalian development

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Temporal and spatial association of histone H2A variant hv1 with transcriptionally competent chromatin during nuclear development in Tetrahymena thermophila

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Histone H2A.Z acetylation modulates an essential charge patch

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Histone H2A.Z is widely but nonrandomly distributed in chromosomes of Drosophila melanogaster

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Crystal structure of a nucleosome core particle containing the variant histone H2A.Z

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Characterization of the stability and folding of H2A.Z chromatin particles: implications for transcriptional activation

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A histone variant, Htz1p, and a Sir1p-like protein, Esc2p, mediate silencing at HMR.

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H2A.Z is required for global chromatin integrity and for recruitment of RNA polymerase II under specific conditions

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Site- and time-specific gene targeting in the mouse

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AID is required to initiate Nbs1/γ-H2AX focus formation and mutations at sites of class switching

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7 January 2021

UV-induced replication arrest in the xeroderma pigmentosum variant leads to DNA double-strand breaks, γ-H2AX formation, and Mre11 relocalization

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Identifiers

DOI

1 reference

Consolidated OpenCitations Corpus – April 2017

1 reference

Consolidated OpenCitations Corpus – April 2017

PubMed publication ID

11893489

1 reference

Consolidated OpenCitations Corpus – April 2017