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    Shedding a Light on Dark Genes: A Comparative Expression Study of PRR12 Orthologues during Zebrafish Development

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    Haploinsufficiency of the PRR12 gene is implicated in a human neuro-ocular syndrome. Although identified as a nuclear protein highly expressed in the embryonic mouse brain, PRR12 molecular function remains elusive. This study explores the spatio-temporal expression of zebrafish PRR12 co-orthologs, prr12a and prr12b, as a first step to elucidate their function. In silico analysis reveals high evolutionary conservation in the DNA-interacting domains for both orthologs, with significant syntenic conservation observed for the prr12b locus. In situ hybridization and RT-qPCR analyses on zebrafish embryos and larvae reveal distinct expression patterns: prr12a is expressed early in zygotic development, mainly in the central nervous system, while prr12b expression initiates during gastrulation, localizing later to dopaminergic telencephalic and diencephalic cell clusters. Both transcripts are enriched in the ganglion cell and inner neural layers of the 72 hpf retina, with prr12b widely distributed in the ciliary marginal zone. In the adult brain, prr12a and prr12b are found in the cerebellum, amygdala and ventral telencephalon, which represent the main areas affected in autistic patients. Overall, this study suggests PRR12's potential involvement in eye and brain development, laying the groundwork for further investigations into PRR12-related neurobehavioral disorders

    Genetic Manipulation of Murine Retinal Stem Cells

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    http://hdl.handle.net/20.500.11768/9675

    Dicer inactivation causes heterochronic retinogenesis in Xenopus laevis

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    Maturation of miRNAs by dicer is required in vertebrates for normal neural development. Here we report that dicer inactivation in Xenopus affects cell cycle progression, survival and timing of the generation of retinal cells, resulting in small retinas with lamination defects. In particular, dicer inactivation delays the exit from the cell cycle and the translation of key genes of late neurogenesis, highlighting a crucial role of miRNAs in retinal development

    RNA binding properties and evolutionary conservation of the Xenopus multifinger protein Xfin

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    Xfin is a Xenopus zinc finger protein which is expressed in the cytoplasm of the oocyte and throughout embryogenesis, as well as in the cytoplasm of some specific and highly differentiated cell types (De Lucchini et al., Mech. Dev. 36, 31-40, 1991). In this paper we present a characterization of some structural features of the protein and of its nucleic acid binding properties. We found that Xfin is a phosphoprotein, is present in the soluble fraction of the cytoplasm, and is actively phosphorylated in cytosolic extracts. Several putative phosphorylation sites are present in the cDNA-derived protein sequence, mostly located at specific positions within the Zn-fingers. In an in vitro assay a fusion protein containing part of the finger region of Xfin exhibits specific binding to a poly (G) RNA homopolymer, while it does not bind DNA. The RNA binding activity of the protein is significantly enhanced by phosphorylation. A putative Xfin homolog, which appears to be evolutionarily conserved with regard to size, cytoplasmic expression and antigenic specificity, is present in representatives of five Vertebrate classes. Taken together, these results may suggest that, by virtue of its RNA binding activity modulated through phosphorylation, Xfin could serve some evolutionarily conserved function in post-transcriptional regulation processes
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