Structure and expression of histone H3.3 genes in<i>Drosophila melanogaster</i>and<i>Drosophila hydei</i>

Akhmanova, Anna; Bindels, Petra; Xu, Jie; Miedema, Koos; Kremer, Hannie; Hennig, Wolfgang

doi:10.1139/g95-075

Cited by 59 publications

(70 citation statements)

References 39 publications

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“…The Drosophila genome encompasses two single-copy genes, H3.3A and H3.3B, which code for the same protein. H3.3 is highly expressed in mitotic, meiotic, and postmeiotic male germ cells, probably reflecting high transcriptional activity (45)(46)(47). Interestingly, high dlp expression levels are observed in primary spermatocytes, in meiotic spermatocytes, and also in the germinal vesicle, suggesting that it may have important functions during the development of germ cells.…”

Section: Discussionmentioning

confidence: 99%

The Drosophila DAXX-Like Protein (DLP) Cooperates with ASF1 for H3.3 Deposition and Heterochromatin Formation

Fromental-Ramain

Ramain

Hamiche

2017

Molecular and Cellular Biology

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Histone variants are nonallelic isoforms of canonical histones, and they are deposited, in contrast to canonical histones, in a replication-independent (RI) manner. RI deposition of H3.3, a histone variant from the H3.3 family, is mediated in mammals by distinct pathways involving either the histone regulator A (HIRA) complex or the death-associated protein (DAXX)/␣-thalassemia X-linked mental retardation protein (ATRX) complex. Here, we investigated the function of the Drosophila DAXX-like protein (DLP) by using both fly genetic approaches and protein biochemistry. DLP specifically interacts with H3.3 and shows a prominent localization on the base of the X chromosome, where it appears to act in concert with XNP, the Drosophila homolog of ATRX, in heterochromatin assembly and maintenance. The functional association between DLP and XNP is further supported by a series of experiments that illustrate genetic interactions and the DLP-XNP-dependent localization of specific chromosomal proteins. In addition, DLP both participates in the RI deposition of H3.3 and associates with anti-silencing factor 1 (ASF1). We suggest, in agreement with a recently proposed model, that DLP and ASF1 are part of a predeposition complex, which is recruited by XNP and is necessary to prevent DNA exposure in the nucleus.KEYWORDS DLP, heterochromatin, histone variant, H3.3, XNP, ASF1 I n the nucleus, DNA is packaged under the form of chromatin. The basic repeating unit of chromatin is the nucleosome, and the nucleosome core particle consists of approximately 146 bp of DNA wrapped around a histone octamer composed of two copies of each of the histones H2A, H2B, H3, and H4. (1, 2). Gene-rich domains are packaged into euchromatin, which is decondensed in interphase nuclei and is enriched for histone modifications characteristic of transcriptionally active regions. Moreover, euchromatin often exhibits high DNA accessibility. In contrast, gene-poor domains and repetitive sequences are packaged into condensed heterochromatin that carries histone modifications associated with transcriptional repression.In addition to the canonical core histones, cells express nonallelic-isoform histone variants (3). Histone variants have emerged as essential contributors to the regulation of chromatin structure, and they are involved in multiple processes, including chromatin stability, DNA repair, and transcriptional regulation. Canonical histones are almost exclusively expressed during the S phase of the cell cycle and are incorporated into chromatin in a DNA replication-dependent fashion, whereas replication-independent (RI) histone variants are expressed throughout the cell cycle.One of the best-studied histone variants is H3.3, which can replace the major species H3 (4). H3.3 is expressed and incorporated at all phases of the cell cycle (5). The available data suggest that H3.3 is a marker of active chromatin and associated with the

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Section: Discussionmentioning

confidence: 99%

The Drosophila DAXX-Like Protein (DLP) Cooperates with ASF1 for H3.3 Deposition and Heterochromatin Formation

Fromental-Ramain

Ramain

Hamiche

2017

Molecular and Cellular Biology

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“…In addition, they often possess introns, and their mRNAs are polyadenylated. In mouse, human and Drosophila, two H3.3 genes (H3.3A and H3.3B) encode the same conserved H3.3 protein, but have distinct untranslated regions [16][17][18]. They are expressed throughout the cell cycle, in quiescence, and are enriched in various stages of differentiation compared with their canonical counterparts [17][18][19][20].…”

Section: H33 Properties Compared With Its Canonical Counterpartsmentioning

confidence: 99%

The double face of the histone variant H3.3

Szenker¹,

Ray-Gallet²,

Almouzni³

2011

Cell Res

325

308

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Histone proteins wrap DNA to form nucleosome particles that compact eukaryotic genomes while still allowing access for cellular processes such as transcription, replication and DNA repair. Histones exist as different variants that have evolved crucial roles in specialized functions in addition to their fundamental role in packaging DNA. H3.3 -a conserved histone variant that is structurally very close to the canonical histone H3 -has been associated with active transcription. Furthermore, its role in histone replacement at active genes and promoters is highly conserved and has been proposed to participate in the epigenetic transmission of active chromatin states. Unexpectedly, recent data have revealed accumulation of this specific variant at silent loci in pericentric heterochromatin and telomeres, raising questions concerning the actual function of H3.3. In this review, we describe the known properties of H3.3 and the current view concerning its incorporation modes involving particular histone chaperones. Finally, we discuss the functional significance of the use of this H3 variant, in particular during germline formation and early development in different species.

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“…The following gene-specific primers were used (the part of the primer, which is present in the corresponding gene, is underlined; see also Fig. 2): histone H2B, S'TATCTAGACCAA-GTCGGGAGATCCAAAC ; histone H3,Y-GATGATCACGGC-ATTAACTTGC ; histone H4, S-GATGATCACAGCCATGGA-TGTTGT ; histone H3.3A, S'-CAGGATCCGATAAGTAAT-CAATAC (positions 678-695 of the D. melanogaster histone H3.3A mRNA, Akhmanova et al, 1995). PCR products were separated on 2% or 3% agarose minigels and in some cases analysed by southern blotting.…”

Section: Determination Of Polyadenylation Sites By Rt-pcrmentioning

confidence: 99%

Two Types of Polyadenated mRNAs are Synthesized from Drosophila Replication‐Dependent Histone Genes

Akhmanova¹,

Miedema²,

Kremer³

et al. 1997

European Journal of Biochemistry

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The polyadenylation of replication-dependent histone H2B, H 3 and H4 mRNAs in Drosophilu melanoguster was analysed. Two types of mRNAs, containing a poly(A) tail, can be detected in addition to non-polyadenylated messengers, which represent the majority of replication-dependent histone mRNAs. Firstly, conventional polyadenylation signals, localized downstream from the stem-loop region, are used to produce polyadenylated mRNAs. The messengers of this type, generated from the D. melanogaster H2B gene, are preferentially synthesized in the testis of the fly. Secondly, a distinct type of polyadenylated histone mRNA has been identified. This mRNA, which is present in many different tissues and constitutes a minor part of the total histone mRNA pool, contains a short poly(A) tail, added to the end of the 3' terminal stem-loop structure, which is in most cases lacking several nucleotides from its 3' end. The sites of polyadenylation within the stem-loop are not preceded by a nornial polyadenylation signal. The possible functions of the polyadenylated histone transcripts are discussed.

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Structure and expression of histone H3.3 genes inDrosophila melanogasterandDrosophila hydei

Cited by 59 publications

References 39 publications

The Drosophila DAXX-Like Protein (DLP) Cooperates with ASF1 for H3.3 Deposition and Heterochromatin Formation

The Drosophila DAXX-Like Protein (DLP) Cooperates with ASF1 for H3.3 Deposition and Heterochromatin Formation

The double face of the histone variant H3.3

Two Types of Polyadenated mRNAs are Synthesized from Drosophila Replication‐Dependent Histone Genes

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