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dc.contributor.authorGómez-Saldívar, Georgina-
dc.contributor.authorGonzález-Aguilera, Cristina-
dc.contributor.authorAskjaer, Peter-
dc.date.accessioned2016-03-16T12:37:25Z-
dc.date.available2016-03-16T12:37:25Z-
dc.date.issued2014-
dc.identifier.citation19th International C. elegans Meeting (2013)-
dc.identifier.urihttp://hdl.handle.net/10261/130189-
dc.descriptionResumen 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.-
dc.description.abstractMEL-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.-
dc.rightsclosedAccess-
dc.titleFunctional dissection of MEL-28, a chromatin-binding protein with essential roles in nuclear envelope function and chromosome segregation-
dc.typepóster de congreso-
dc.date.updated2016-03-16T12:37:25Z-
dc.description.versionPeer Reviewed-
dc.language.rfc3066eng-
dc.relation.csic-
Appears in Collections:(CABD) Comunicaciones congresos
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