Reference : Dynamic Nucleocytoplasmic Shuttling of an Arabidopsis SR Splicing Factor: Role of the RN...
Scientific journals : Article
Life sciences : Genetics & genetic processes
http://hdl.handle.net/2268/40753
Dynamic Nucleocytoplasmic Shuttling of an Arabidopsis SR Splicing Factor: Role of the RNA-Binding Domains
English
Rausin, Glwadys mailto [Université de Liège - ULg > Département des sciences de la vie > Génomique fonctionnelle et imagerie moléculaire végétale >]
Tillemans, Vinciane mailto [Université de Liège - ULg > Département des sciences de la vie > Génomique fonctionnelle et imagerie moléculaire végétale >]
Stankovic, Nancy [Université de Liège - ULg > Département des sciences de la vie > Génomique fonctionnelle et imagerie moléculaire végétale >]
Hanikenne, Marc mailto [Université de Liège - ULg > Département des sciences de la vie > Génomique fonctionnelle et imagerie moléculaire végétale >]
Motte, Patrick mailto [Université de Liège - ULg > Département des sciences de la vie > Génomique fonctionnelle et imagerie moléculaire végétale >]
May-2010
Plant Physiology
American Society of Plant Biologists
153
273-284
Yes (verified by ORBi)
International
0032-0889
1532-2548
Rockville
MD
[en] splicing ; SR protein ; nuclear export
[en] Serine/arginine-rich (SR) proteins are essential nuclear-localized splicing factors. We have investigated the dynamic subcellular distribution of the Arabidopsis (Arabidopsis thaliana) RSZp22 protein, a homolog of the human 9G8 SR factor. Little is known about the determinants underlying the control of plant SR protein dynamics, and so far most studies relied on ectopic transient overexpression. Here, we provide a detailed analysis of the RSZp22 expression profile and describe its nucleocytoplasmic shuttling properties in specific cell types. Comparison of transient ectopic- and stable tissue-specific expression highlights the advantages of both approaches for nuclear protein dynamic studies. By site-directed mutagenesis of RSZp22 RNA-binding sequences, we show that functional RNA recognition motif RNP1 and zinc-knuckle are dispensable for the exclusive protein nuclear localization and speckle-like distribution. Fluorescence resonance energy transfer imaging also revealed that these motifs are implicated in RSZp22 molecular interactions. Furthermore, the RNA-binding motif mutants are defective for their export through the CRM1/XPO1/Exportin-1 receptor pathway but retain nucleocytoplasmic mobility. Moreover, our data suggest that CRM1 is a putative export receptor for mRNPs in plants.
Researchers ; Professionals ; Students
http://hdl.handle.net/2268/40753

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