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Título:	Functional dissection of MEL-28, a chromatin-binding protein with essential roles in nuclear envelope function and chromosome segregation
Autor:	Gómez-Saldívar, Georgina CSIC; González-Aguilera, Cristina CSIC; Askjaer, Peter CSIC ORCID
Fecha de publicación:	2014
Citación:	19th International C. elegans Meeting (2013)
Resumen:	MEL-28/ELYS is a large AT-Hook protein required for the proper structure and function of the nuclear envelope during interphase in nematodes and vertebrates. In addition, MEL-28 has critical roles in chromosome congression and segregation during mitosis. MEL-28 localizes to nuclear pores and chromatin during interphase and shuttles to the kinetochore during cell division. Other than the AT-Hook domains, which suggest that MEL-28 binds DNA directly, primary structure analysis has not revealed functional domains. Biochemical studies have demonstrated that MEL-28 interacts with the NUP107 subcomplex at nuclear pores, but its targeting mechanism to kinetochores is unknown. We are interested in understanding 1) the function and mode of MEL-28 chromatin binding and 2) which regions of the MEL-28 protein are required for its different functions. To this end we have used DamID to define the chromatin regions with which MEL-28 associates. Interestingly, MEL-28 is enriched in active chromatin, suggesting that it may be involved in regulation of gene expression. In addition we are using a structure/function approach to determine which domains of the MEL-28 protein are required for MEL-28 localization and function. We have generated truncated versions of MEL-28 that lack different domains and fused these to GFP to track their localization in live embryos. Biological function of these fusions is evaluated by crossing them into mel-28 mutants and scoring for rescue of embryonic lethality. In doing this we have defined separate domains that are implicated in localization of MEL-28 to the nuclear envelope, chromatin and kinetochores. Surprisingly, we have found that removal of the AT Hooks does not affect MEL-28 localization although it does disrupt MEL-28 function. These studies illuminate the functioning of an essential and conserved protein.
Descripción:	Resumen del póster presentado al 19th International C. elegans Meeting, celebrado en Los Angeles, California (US) del 26 al 30 de junio de 2013.-- et al.
URI:	http://hdl.handle.net/10261/130189
Aparece en las colecciones:	(CABD) Comunicaciones congresos