Implication of a 5′ coding sequence in targeting maternal mRNA to the Drosophila oocyte

Capri, Michèle; Santoni, Marie-Josée; Thomas-Delaage, Michèle; Aı̈t-Ahmed, Ounissa

doi:10.1016/s0925-4773(97)00130-5

Cited by 37 publications

(32 citation statements)

References 44 publications

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“…As shown in Fig. 1A, Yem could be detected from as early as region 2a of the germarium, which is in line with its mRNA expression and localization (Capri et al, 1997). The various stages are schematically shown up to mid-prophase in the drawing of Fig.…”

Section: Yem Is a New Synaptonemal-complex-associated Proteinsupporting

confidence: 68%

“…For Yem detection, immunostaining was performed with a polyclonal antibody developed against Yem-a; washing and incubation with fluorescent secondary antibodies were as described previously (Aït-Ahmed et al, 1992;Capri et al, 1997;Meyer et al, 2010). Additional primary antibodies included mouse anti-C(3)G antibody, used at 1:500 (Page and Hawley, 2001), rabbit anti-C(2)M antibody, used at 1:400 , and the monoclonal anti-HA tag antibody, used at 1:200 (Sigma).…”

Section: Methodsmentioning

confidence: 99%

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Drosophila Yemanuclein is a cohesin and synaptonemal complex associated protein

Meyer

Algazeery

Capri

et al. 2014

Journal of Cell Science

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Meiosis is characterized by two chromosome segregation rounds (meiosis I and II), which follow a single round of DNA replication, resulting in haploid genome formation. Chromosome reduction occurs at meiosis I. It relies on key structures, such as chiasmata, which are formed by repair of double-strand breaks (DSBs) between the homologous chromatids. In turn, to allow for segregation of homologs, chiasmata rely on the maintenance of sister chromatid cohesion. In most species, chiasma formation requires the prior synapsis of homologous chromosome axes, which is mediated by the synaptonemal complex, a tripartite proteinaceous structure specific to prophase I of meiosis. Yemanuclein (Yem) is a maternal factor that is crucial for sexual reproduction. It is required in the zygote for chromatin assembly of the male pronucleus, where it acts as a histone H3.3 chaperone in complex with Hira. We report here that Yem associates with the synaptonemal complex and the cohesin complex. A genetic interaction between yem 1 (V478E) and the Spo11 homolog mei-W68, modified a yem 1 dominant effect on crossover distribution, suggesting that Yem has an early role in meiotic recombination. This is further supported by the impact of yem mutations on DSB kinetics. A Hira mutation gave a similar effect, presumably through disruption of Hira-Yem complex.

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Section: Yem Is a New Synaptonemal-complex-associated Proteinsupporting

confidence: 68%

Section: Methodsmentioning

confidence: 99%

Drosophila Yemanuclein is a cohesin and synaptonemal complex associated protein

Meyer

Algazeery

Capri

et al. 2014

Journal of Cell Science

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“…Immunostaining of testis squashes was performed as described previously (56). Immunostaining of ovaries was performed as described previously (57). Immunostaining of polytene squashes was performed as described previously (58).…”

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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“…The localization of ASH1 mRNA to the yeast bud tip can be mediated by any one of three cis-acting elements; two of these elements are located entirely within the ORF, and the third spans the ORF and the 3Ј UTR (34,35). Other localized mRNAs, namely rat vasopressin precursor and Drosophila gurken and yem-alpha, appear to require a contribution from protein-coding sequences for localization, but such sequences have not been shown to be sufficient to reconstitute the wild-type localization pattern (36)(37)(38)(39). One might expect the presence of mRNA localization elements within the btsz ORF to interfere with its translation.…”

Section: Resultsmentioning

confidence: 99%

The Drosophila synaptotagmin-like protein bitesize is required for growth and has mRNA localization sequences within its open reading frame

Serano

Rubin

2003

Proc. Natl. Acad. Sci. U.S.A.

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The vertebrate synaptotagmin-like protein granuphilin binds to the vesicle-trafficking proteins Rab27a and Munc18 and can modulate exocytosis of insulin-containing secretory granules in pancreatic beta cell lines. Here, we report the molecular and genetic characterization of bitesize, a granuphilin homolog and the only Drosophila synaptotagmin-like protein. Mutations that affect bitesize have reduced cell size and number, resulting in smaller animals that develop slowly. We also show that at least two classes of bitesize transcripts are localized to the apical plasma membrane in polarized epithelial cells. Whereas most cis-acting mRNA localization sequences map to 3 untranslated regions, bitesize contains a 2.2-kb sequence within its ORF that is necessary and sufficient for apical localization. Thus, we have found that bitesize is a metazoan example of a transcript for which all identifiable mRNA localization sequences are contained within the protein-coding region.

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Implication of a 5′ coding sequence in targeting maternal mRNA to the Drosophila oocyte

Cited by 37 publications

References 44 publications

Drosophila Yemanuclein is a cohesin and synaptonemal complex associated protein

Drosophila Yemanuclein is a cohesin and synaptonemal complex associated protein

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

The Drosophila synaptotagmin-like protein bitesize is required for growth and has mRNA localization sequences within its open reading frame

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