INVESTIGADORES
CORIGLIANO Mariana Georgina
artículos
Título:
Heat treatment alleviates the growth and photosynthetic impairment of transplastomic plants expressing Leishmania infantum Hsp 83-Toxoplasma gondii SAG1 fusion protein
Autor/es:
CORIGLIANO, MARIANA G; ALBARRACÍN, ROMINA M; VILAS, JUAN M; SÁNCHEZ LÓPEZ, EDWIN F; BENGOA LUONI, SOFIA A; BIN, DENG; FARRAN, INMACULADA; VERAMENDI, JON; MAIALE, SANTIAGO J; SANDER, VALERIA A; CLEMENTE, MARINA
Revista:
PLANT SCIENCE
Editorial:
ELSEVIER IRELAND LTD
Referencias:
Lugar: Amsterdam; Año: 2019
ISSN:
0168-9452
Resumen:
Previously,we showed that transplastomic tobacco plants expressing the LiHsp83-SAG1 fusionprotein displayed a chlorotic phenotype and growth retardation, while plantsexpressing the SAG1 and GRA4 antigens alone did not. We conducted acomprehensive examination of the metabolic and photosynthetic parameters thatcould be affecting the normal growth of LiHsp83-SAG1 plants in order tounderstand the origin of these pleiotropic effects. These plants presented allphotosynthetic pigments and parameters related to PSII efficiency significantlydiminished. However, the expression of CHLI,RSSU and LHCa/b genes did not show significant differences betweenLiHsp83-SAG1 and control plants. Total protein, starch, and soluble sugarcontents were also greatly reduced in LiHsp83-SAG1 plants. Since Hsp90s are constitutivelyexpressed at much higher concentrations at high temperatures, we tested if thefitness of LiHsp83-SAG1 over-expressing LiHsp83 would improve after heattreatment. LiHsp83-SAG1 plants showed an important alleviation of theirphenotype and an evident recovery of the PSII function. As far as we know, thisis the first report where it is demonstrated that a transplastomic lineperforms much better at higher temperatures. Finally, we detected thatLiHsp83-SAG1 protein could be binding to key photosynthesis-related proteins at37 °C. Our results suggest that the excess of this molecular chaperone could benefit the plant in a possible heat shock and preventthe expected denaturation of proteins. However, the LiHsp83-SAG1 proteincontent was weakly decreased in heat-treated plants. Therefore, we cannot ruleout that the alleviation observed at 37 ºC may be partially due to a reductionof the levels of the recombinant protein.