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Title

The role of nuclear envelope proteins MEL-28 and BAF-1 in chromatin organisation

AuthorsRomero Bueno, Raquel; Gómez-Saldívar, Georgina ; Dobrzynska, Agnieszka ; Rojas, Marta; Ayuso, Cristina ; Riedel, Meister, Peter; Christian ; Askjaer, Peter
Issue Date28-Mar-2019
CitationVII Spanish Worm Meeting (2019)
AbstractThe nuclear envelope (NE) affects multiple genomic activities through chromosome organisation and nucleocytoplasmic transport. Our aim is to study the chromatin organisation properties of two NE components: MEL-28 and BAF-1. The nuclear pore protein MEL-28/ELYS plays a critical role in NPC assembly through recruitment of the NUP107-160 subcomplex and is required for correct segregation of meiotic and mitotic chromosomes. However, MEL-28 is also expressed in post-mitotic cells, suggesting that it might have additional functions. In support of this, we have observed that mel-28 mutants have a delayed larval development and dramatically reduced lifespan, both in the presence of proliferating germ cells and in sterile glp-4 animals. A significant fraction of MEL-28 localises in the nucleoplasm, suggesting that MEL-28 might be directly involved in control of gene expression. To identify genes potentially regulated by MEL-28 we performed DamID experiments. This revealed that MEL-28¿s binding profile is different from those of others NE proteins (NPP-22/NDC1, LMN-1/lamin and EMR-1/emerin), associating more frequently with active chromatin. We are currently studying the effect of MEL-28 depletion on nuclear organization and gene expression. Using Bimolecular Fluorescence Complementation, we discovered Barrier to Autointegration Factor (BAF-1) as a novel MEL-28 interaction partner. BAF-1 is a highly conserved chromatin binding protein implicated in NE breakdown and assembly as well as chromatin compaction. Its NE localisation is interdependent of lamins and LEM-domain proteins, but, similarly to MEL-28, BAF-1 is also present in the nucleoplasm. Mutation of BAF in humans causes Nestor-Guillermo Progeria Syndrome (NGPS) potentially because of the disruption of binding to lamin. To explore C. elegans as model for this devastating disease, we have generated a baf-1 strain that mimics the human NGPS mutation. Our preliminary analyses reveal that C. elegans mutants are hypersensitive to NE perturbations, which affect nuclear morphology, chromosome segregation and embryonic viability. This serves as initial validation of the model and we expect to gain further insight to the mechanisms of NGPS.
DescriptionResumen del trabajo presentado en el VII Spanish Worm Meeting, celebrado en Barcelona (España), los días 28 y 29 de marzo de 2019
URIhttp://hdl.handle.net/10261/210642
Appears in Collections:(CABD) Comunicaciones congresos
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