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Estructura molecular de dos enzimas, FBPase (izq.) y SBPase (dcha.), de «Physcomitrella».. © Universidad de Friburgo (Alemania), Universidad de Lorena (Francia), Oliver Einsle, Thomas Roret

El sorprendente origen de la fotosíntesis

La fotosíntesis, que consiste en la conversión de la luz del sol en energía química, es uno de los procesos biológicos más importantes de la Tierra. Un equipo internacional de investigadores del INRA y de las universidades de Lorena (Francia), Friburgo (Alemania) y Berkeley (EE. UU.) ha descubierto el sorprendente origen de este proceso. Utilizando como modelo el musgo Physcomitrella patens, los investigadores han demostrado que durante la evolución algunos organismos que pertenecen a dos tipos diferentes de organismos vivos han contribuido a la creación del sistema biológico fijador del dióxido de carbono. Este descubrimiento, que ha sido publicado en la revista «Proceedings of the National Academy of Sciences of the United States of America» (PNAS), es el resultado de estudios que empezaron hace más de cuarenta años.

Actualización: 30/06/2017
Publicación: 13/06/2016

Los vegetales terrestres, las algas y ciertas bacterias realizan la fotosíntesis oxigénica, lo que supone una liberación de oxígeno y la fijación de dióxido de carbono. El CO2 fijado de este modo se utiliza para la síntesis de azúcares. La fotosíntesis es fundamental en la energía y la materia orgánica de la Tierra. También tiene una función clave para que se mantenga constante la tasa de oxígeno y se reduzca el contenido de CO2 —un importante gas de efecto invernadero—, en la atmósfera terrestre.

 corre a cargo de algunos cientos de enzimas. La eficacia de esa fijación condiciona especialmente los rendimientos agronómicos. Dos de estas enzimas, la fructosa-1,6-bisfosfatasa (FBPasa) y la sedoheptulosa-bisfosfatasa (SBPasa), son objeto de estudio desde hace cuarenta años. Gracias a análisis bioquímicos y genéticos llevados a cabo con el musgo Physcomitrella patens, los investigadores han demostrado en este estudio su estructura molecular y su modo de acción, y han descifrado la evolución del sistema fotosintético.

Sorprendentemente, las dos enzimas aisladas a partir del musgo son bastante parecidas en su modo de acción, pero provienen de organismos vivos de dos tipos diferentes. El análisis del origen de los dos genes que codifican estas enzimas indica que una proviene de bacterias no fotosintéticas y la otra de organismos ancestrales llamados arqueas. Estos resultados aportan datos sorprendentes sobre el origen de los sistemas fotosintéticos, que aparentemente reposan sobre un conjunto de genes adquiridos a partir de organismos más primitivos no fotosintéticos, adaptados después al funcionamiento particular de los organismos que realizan la fotosíntesis oxigénica. Con estos estudios, se mejoran los conocimientos sobre el funcionamiento y la regulación de la fotosíntesis así como sobre el control de la productividad vegetal.

Estructura molecular de dos enzimas, FBPasa (izq.) y SBPasa (dcha.), de «Physcomitrella».. © Universidad de Friburgo (Alemania), Universidad de Lorena (Francia), Oliver Einsle, Thomas Roret
Estructura molecular de dos enzimas, FBPasa (izq.) y SBPasa (dcha.), de «Physcomitrella». © Universidad de Friburgo (Alemania), Universidad de Lorena (Francia), Oliver Einsle, Thomas Roret

Los resultados de este estudio provienen principalmente de la colaboración entre la Unidad Mixta de Investigación de Interacciones entre Árboles y Microorganismos del INRA y la Universidad de Lorena, por una parte, y el Laboratorio de Biotecnología Vegetal de la Facultad de Biología y el de Bioquímica de la Facultad de Química y Farmacia de la Universidad de Friburgo, por otra. También se ha comenzado a colaborar con un laboratorio del Instituto de Biología Físico-Química (IBPC) de París y el Departamento de Biología Vegetal y Microbiana de la Universidad de California en Berkeley.

Este artículo corresponde en gran parte a los estudios de tesis de Désirée Gütle, tutorizados en Nancy y Friburgo, y efectuados gracias a una beca del Ministerio de Investigación de Francia y del Labex ARBRE, y a la Iniciativa de Excelencia de Alemania, que engloba a las estructuras SGCBM, BIOSS, FRIAS de Friburgo y a la Universidad Franco-Alemana.

Contacto
Contacto científico:

  • Jean-Pierre Jacquot (+33 (0) 6 80 72 40 29) Unidad Mixta de Investigación de Interacciones entre Árboles y Microorganismos del INRA y la Universidad de Lorena
Contacto de prensa:
Servicio de Prensa del INRA (+33 (0) 1 42 75 91 86), Fanny Lienhardt, responsable de prensa de la Universidad de Lorena (+33 (0) 3 54 50 54 51)
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Forest, Grassland and Freshwater Ecology
Centro asociado:
Nancy-Lorraine

REFERENCIA

Desirée D. Gütle, Thomas Roret, Stefanie J. Mueller, Jérémy Couturier, Stéphane D. Lemaire, Arnaud Hecker, Tiphaine Dhalleine, Bob B. Buchanan, Ralf Reski, Oliver Einsle, Jean-Pierre Jacquot (2016): Chloroplast FBPase and SPBase are thioredoxin-linked enzymes with similar architecture but different evolutionary histories. Proceedings of the National Academy of Sciences (USA), DOI: 10.1073/pnas.1606241113.