000077640 001__ 77640 000077640 005__ 20190226114803.0 000077640 037__ $$aTAZ-TFG-2018-2789 000077640 041__ $$aeng 000077640 1001_ $$aSabater Royo, Irene 000077640 24200 $$aProteínas G Extra-Largas de Arabidopsis en la homeostasis del fosfato 000077640 24500 $$aArabidopsis Extra-Large G Proteins (XLGs) in phosphate homeostasis 000077640 260__ $$aZaragoza$$bUniversidad de Zaragoza$$c2018 000077640 506__ $$aby-nc-sa$$bCreative Commons$$c3.0$$uhttp://creativecommons.org/licenses/by-nc-sa/3.0/ 000077640 520__ $$aPhosphorus, which is taken up as inorganic phosphate (Pi), is one of the most limiting nutrients for plants. To maintain Pi homeostasis, many proteins (e.g. SPX domain proteins) are involved in signalling pathways to mediate different plant responses. In addition to the canonical heterotrimeric G proteins, the Arabidopsis genome encodes three Gα-like proteins, named Extra-Large G proteins: XLG1, XLG2, and XLG3. This project study the role of XLGs in Pi homeostasis in Arabidopsis thaliana. Analysis of the shoot Pi content showed a decreased accumulation in xlg1-2 and xlg3-2 single mutants, which is more notable in the xlg1-2 xlg3-2 double mutant. Under Pi starvation, the xlg1-2 xlg3-2 double mutant developed longer primary roots compared to wild-type plants, while the single xlg mutants were not significant different. Furthermore, all tested xlg single and double mutants showed a tendency toward increased transcript levels of phosphate starvation induced genes compared to the wild-type. Additionally, yeast two-hybrid assays showed an interaction between SPX proteins and XLG1 and XLG3. AtSPX1, a phosphate-dependent inhibitor of the MYB-type transcription factor Phosphate Starvation Response 1 (PHR1), interacts with both AtXLG1 and AtXLG3. However, AtSPX-MFS1, a vacuolar transporter that mediates phosphate storage, only interacts with AtXLG3. These results suggest that XLGs proteins may play a role in Pi homeostasis together with SPX proteins. To test for brassinosteroid related phenotypes, plants were treated with the brassinosteroid biosynthesis inhibitor brassinazole (BRZ). The xlg3-2 mutant showed a decreased in hypocotyl length compared to wild-type, while the xlg1-2 and spx1-1 mutants did not. The xlg1-2 xlg3-2 double mutant showed the same tendency as the xlg3-2, suggesting that the phenotype is caused by the XLG3 mutation. Taken together, these results suggest that XLGs proteins may be involved in different signaling pathways. Nevertheless, little is known about these signalling proteins, and further studies are needed to define how they work. 000077640 521__ $$aGraduado en Biotecnología 000077640 540__ $$aDerechos regulados por licencia Creative Commons 000077640 700__ $$aRied, Martina$$edir. 000077640 700__ $$aHothorn, Michael$$edir. 000077640 7102_ $$aUniversidad de Zaragoza$$bBioquímica y Biología Molecular y Celular$$c 000077640 8560_ $$f701827@celes.unizar.es 000077640 8564_ $$s1300020$$uhttps://zaguan.unizar.es/record/77640/files/TAZ-TFG-2018-2789.pdf$$yMemoria (eng) 000077640 8564_ $$s225284$$uhttps://zaguan.unizar.es/record/77640/files/TAZ-TFG-2018-2789_ANE.pdf$$yAnexos (eng) 000077640 909CO $$ooai:zaguan.unizar.es:77640$$pdriver$$ptrabajos-fin-grado 000077640 950__ $$a 000077640 951__ $$adeposita:2019-02-26 000077640 980__ $$aTAZ$$bTFG$$cCIEN 000077640 999__ $$a20180711092151.CREATION_DATE