Towards an understanding of photosynthetic acclimation.
It has long been recognized that higher plants vary the composition and organization of the photosynthetic apparatus in response to the prevailing environmental conditions, with particular attention being paid to the responses to incident light. Under high light conditions there are increases in the amounts of photosystems, electron transport and ATP synthase complexes, and enzymes of the Calvin-Benson cycle; conversely, under low light there is an increase in the relative amounts of light-harvesting complexes (LHC) and in the stacking of thylakoid membranes to form grana. It is believed that these changes are of adaptive significance, and in a few instances evidence has been provided that this is indeed the case; an increase in photosynthetic capacity reduces susceptibility to photodamage, while changes in photosystem stoichiometry serve to optimize light utilization. By contrast, the potential benefit to the plant of other changes in chloroplast composition, such as in the levels of LHC, is far less clear. It is also believed that redox signals derived from photosynthetic electron transport play an important regulatory role in acclimation. However, while there is convincing evidence that such redox signals modulate the expression of many plastidic and nuclear genes encoding photosynthetic components, there is little to demonstrate that such changes are responsible for regulating chloroplast composition. This review discusses the evidence that particular aspects of acclimation are advantageous to the plant, and highlights the significant gaps in our understanding of the mechanisms underlying acclimation.
Walters
Robin G
RG
Department of Plant Sciences, University of Oxford, South Parks Road, Oxford OX1 3RB, UK. robin.walters@plants.ox.ac.uk
D000064:Acclimatization / Q000502:physiology*; D002736:Chloroplasts / Q000502:physiology; D004777:Environment; D008027:Light; D010788:Photosynthesis / Q000502:physiology*; D018521:Plant Physiological Phenomena; D015398:Signal Transduction / Q000502:physiology