IQUIFIB   02644
INSTITUTO DE QUIMICA Y FISICOQUIMICA BIOLOGICAS "PROF. ALEJANDRO C. PALADINI"
Unidad Ejecutora - UE
congresos y reuniones científicas
Título:
Biophysical characterization of Medicago truncatula PIP aquaporins
Autor/es:
AGUSTINA CANESSA FORTUNA; ROMINA FRARE; NICOLAS AYUB; VICTORIA VITALI; FLORENCIA SCOCHERA; GABRIELA SOTO; FLORENCIA GIORGETTO; LUIS BREDESTON; KARINA ALLEVA
Lugar:
San Luis
Reunión:
Congreso; XLVIII Reunión Anual de la Sociedad Argentina de Biofísica; 2019
Institución organizadora:
Sociedad Argentina de Biofísica
Resumen:
Legumes are important cultivated species in part due to symbiotic nitrogen fixation byrhizobia. Medicago truncatula is the closest plant model to alfalfa. The colonization oflegumes roots triggers a development program that forms nitrogen-fixing nodules.Among all the transmembrane proteins of the legume nodules so far described, therecurrence of members of the aquaporin family is striking. In this work we present theprogress achieved in the biophysical characterization Medicago truncatula PIPaquaporins. First, by means of cloning, heterologous expression in Xenopus laevisoocytes and water transport assays, we characterized the functional consequences ofthe interaction among two PIP2 (here named MtPIP2A and MtPIP2B) and two PIP1 (herenamed MtPIP1A and MtPIP1B). We found that not all pairs PIP2-PIP1 present the same pHgating profile, showing the amplification of the biological response that can be obtainedby these kind of interactions in a cell. Then, we explored the expression profile of each ofthese four PIP in whole plant by analysis of available transcriptomic data to know if theinteractions found are plausible in vivo. Finally, we present the first steps in the GFPbasedoptimization scheme followed to achieve the overexpression and purification ofthese channels in S. cerevisiae. These biophysical studies not only contribute to theunderstanding of PIP biological function in legumes but also are an opportunity toexplore the complex mechanism of hetero-oligomerization and pH gating showed by thePIP aquaporin family of channels.