Dynamics of Photosystem Stoichiometry Adjustment by Light Quality in Chloroplasts
Author(s) -
J. H. Kim,
R. E. Glick,
Anastasios Melis
Publication year - 1993
Publication title -
plant physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.554
H-Index - 312
eISSN - 1532-2548
pISSN - 0032-0889
DOI - 10.1104/pp.102.1.181
Subject(s) - p700 , photosystem ii , photosystem i , plastoquinone , photosynthetic reaction centre , light harvesting complexes of green plants , hordeum vulgare , thylakoid , photosystem , chloroplast , photosynthesis , cytochrome b6f complex , biology , electron transport chain , chloroplast stroma , chlorophyll , biophysics , chemistry , photochemistry , botany , biochemistry , poaceae , gene
Long-term imbalance in light absorption and electron transport by photosystem I (PSI) and photosystem II (PSII) in chloroplasts brings about changes in the composition, structure, and function of thylakoid membranes. The response entails adjustment in the photosystem ratio, which is optimized to help the plant retain a high quantum efficiency of photosynthesis (W.S. Chow, A. Melis, J.M. Anderson [1990] Proc Nat Acad Sci USA 87: 7502-7506). The dynamics of photosystem ratio adjustment were investigated upon the transfer of pea {Pisum sativum} plants from a predominantly PSI-light to a predominantly PSII-light environment and vice versa. The concentration of functional components (primary electron accepting plastoquinone of PSII [QA], P700) and that of constituent proteins were monitored during acclimation by A difference spectrophotometry and immunoblot analysis, respectively. Fully reversible changes in photosystem ratio occurred with a half-time of about 20 h. They involved closely coordinated changes in the concentration of the QA, reaction center protein D1, D2, and the 9-kD apoprotein of the cytochrome b559 for PSII. Similarly, closely coordinated changes in the relative concentration of P700 and reaction center proteins of PSI were observed. The level of chlorophyll b and that of the light-harvesting complex II changed in accordance with the concentration of PSII in the acclimating thylakoids. Overall, adjustments in the photosystem ratio in response to PSI- or PSII-light conditions appeared to be a well-coordinated reaction in the chloroplast. The response was absent in the chlorophyll b-less chlorina f2 mutant of barley (Hordeum vulgare) and in a phycobilisomeless mutant of Agmenellum quadruplicatum, suggesting that photosystem accessory pigments act as the light-quality perception molecules and that PSI and PSII themselves play a role in the signal transduction pathway.
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