Compensatory Alterations in the Photochemical Apparatus of a Photoregulatory, Chlorophyll b-Deficient Mutant of Maize
Ben Greene, L. Andrew Staehelin, Anastasios Melis
Abstract
Ben Greene, L. Andrew Staehelin, Anastasios Melis
Abstract
Characterization of the functional organization of the photochemical apparatus in the light sensitive chlorophyll b-deficient oil yellow-yellow green (OY-YG) mutant of maize (Zea mays) is presented. Spectrophotometric and kinetic analysis revealed substantially lower amounts of the light harvesting complex of photosystem II (LHCII-peripheral) in high light-grown OY-YG thylakoids. However, accumulation of a tightly bound LHCII appears unaffected by the lesion. Changes in photosystem (PS) stoichiometry include lower amounts of PSII with characteristic fast kinetics (PSII(alpha)) and a substantial accumulation of PSII centers with characteristic slow kinetics (PSII(beta)) in the thylakoid membrane of the OY-YG mutant. Thus, PSII(beta) is the dominant photosystem in the mutant chloroplasts. In contrast to wild type, roughly 80% of the mutant PSII(beta) centers are functionally coupled to the plastoquinone pool and are probably localized in the appressed regions of the thylakoid membrane. These centers, designated PSII(beta)-Q(B)-reducing (Q(B) being the secondary electron quinone acceptor of PSII), are clearly distinct from the typical PSII(beta)-Q(B)-nonreducing centers found in the stroma lamellae of wild-type chloroplasts. It is concluded that the observed changes in the stoichiometry of electron-transport complexes reflect the existence of a regulatory mechanism for the adjustment of photosystem stoichiometry in chloroplasts designed to correct any imbalance in light absorption by the two photosystems.
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Characterization of the functional organization of the photochemical apparatus in the light sensitive chlorophyll b-deficient oil yellow-yellow green (OY-YG) mutant of maize (Zea mays) is presented. Spectrophotometric and kinetic analysis revealed substantially lower amounts of the light harvesting complex of photosystem II (LHCII-peripheral) in high light-grown OY-YG thylakoids. However, accumulation of a tightly bound LHCII appears unaffected by the lesion. Changes in photosystem (PS) stoichiometry include lower amounts of PSII with characteristic fast kinetics (PSII(alpha)) and a substantial accumulation of PSII centers with characteristic slow kinetics (PSII(beta)) in the thylakoid membrane of the OY-YG mutant. Thus, PSII(beta) is the dominant photosystem in the mutant chloroplasts. In contrast to wild type, roughly 80% of the mutant PSII(beta) centers are functionally coupled to the plastoquinone pool and are probably localized in the appressed regions of the thylakoid membrane. These centers, designated PSII(beta)-Q(B)-reducing (Q(B) being the secondary electron quinone acceptor of PSII), are clearly distinct from the typical PSII(beta)-Q(B)-nonreducing centers found in the stroma lamellae of wild-type chloroplasts. It is concluded that the observed changes in the stoichiometry of electron-transport complexes reflect the existence of a regulatory mechanism for the adjustment of photosystem stoichiometry in chloroplasts designed to correct any imbalance in light absorption by the two photosystems.
Key concepts: Thylakoid, Photosystem, Photosystem II, Plastoquinone, Chloroplast, Photosystem I, Photosynthesis, Light-harvesting complexes of green plants