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Successful reproduction requires the function of Arabidopsis Yellow Stripe-Like1 and Yellow Stripe-Like3 metal-nicotianamine transporters in both vegetative and reproductive structures.
Chu, Heng-Hsuan; Chiecko, Jeff; Punshon, Tracy; Lanzirotti, Antonio; Lahner, Brett; Salt, David E; Walker, Elsbeth L.
Afiliación
  • Chu HH; Plant Biology Graduate Program, University of Massachusetts, Amherst, Massachusetts 01003, USA.
Plant Physiol ; 154(1): 197-210, 2010 Sep.
Article en En | MEDLINE | ID: mdl-20625001
ABSTRACT
Several members of the Yellow Stripe-Like (YSL) family of proteins are transporters of metals that are bound to the metal chelator nicotianamine or the related set of mugineic acid family chelators known as phytosiderophores. Here, we examine the physiological functions of three closely related Arabidopsis (Arabidopsis thaliana) YSL family members, AtYSL1, AtYSL2, and AtYSL3, to elucidate their role(s) in the allocation of metals into various organs of Arabidopsis. We show that AtYSL3 and AtYSL1 are localized to the plasma membrane and function as iron transporters in yeast functional complementation assays. By using inflorescence grafting, we show that AtYSL1 and AtYSL3 have dual roles in reproduction their activity in the leaves is required for normal fertility and normal seed development, while activity in the inflorescences themselves is required for proper loading of metals into the seeds. We further demonstrate that the AtYSL1 and AtYSL2 proteins, when expressed from the AtYSL3 promoter, can only partially rescue the phenotypes of a ysl1ysl3 double mutant, suggesting that although these three YSL transporters are closely related and have similar patterns of expression, they have distinct activities in planta. In particular, neither AtYSL1 nor AtYSL2 is able to functionally complement the reproductive defects exhibited by ysl1ysl3 double mutant plants.
Asunto(s)

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Proteínas de Transporte de Membrana / Ácido Azetidinocarboxílico / Arabidopsis / Proteínas de Arabidopsis / Flores / Metales Idioma: En Revista: Plant Physiol Año: 2010 Tipo del documento: Article País de afiliación: Estados Unidos

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Proteínas de Transporte de Membrana / Ácido Azetidinocarboxílico / Arabidopsis / Proteínas de Arabidopsis / Flores / Metales Idioma: En Revista: Plant Physiol Año: 2010 Tipo del documento: Article País de afiliación: Estados Unidos