期刊
NEW PHYTOLOGIST
卷 185, 期 1, 页码 173-188出版社
WILEY
DOI: 10.1111/j.1469-8137.2009.03068.x
关键词
light acclimation; protein turnover; regulation of photosynthesis for nitrogen fixation; reversible phycobiliprotein coupling; spectrally resolved fluorescence kinetics; Trichodesmium
资金
- Deutsche Forschungsgemeinschaft [KU 1495/2, AD-92/7-3]
- Konstanz University
- Ministry of Education, Youth and Sports of the Czech Republic [MSM 6007665801]
- Grant Agency of the Czech Republic [GACR 206/08/1683]
P>As the nonheterocystous diazotrophic cyanobacterium Trichodesmium lives both at the ocean surface and deep in the water column, it has to acclimate to vastly different irradiances. Here, we investigate its strategy of light acclimation in several ways. In this study, we used spectrally resolved fluorescence kinetic microscopy to investigate the biophysics of photosynthesis in individual cells, analysed cell extracts for pigment and phycobiliprotein composition, measured nitrogenase activity and the abundance of key proteins, and assayed protein synthesis/degradation by radioactive labelling. After acclimation to high light, Trichodesmium grew faster at 1000 mu mol m-2 s-1 than at 100 mu mol m-2 s-1. This acclimation was associated with decreasing cell diameter, faster protein turnover, the down-regulation of light-harvesting pigments and the outer part of the phycobiliprotein antenna, the up-regulation of light-protective carotenoids, changes in the coupling of phycobilisomes to the reaction centres and in the coupling of individual phycobiliproteins to the phycobilisomes. The latter was particularly interesting, as it represents an as yet unreported light acclimation strategy. Only in the low light-acclimated culture and only after the onset of actinic light did phycourobilin and phycoerythrin contribute to photochemical fluorescence quenching, showing that these phycobiliproteins may become quickly (in seconds) very closely coupled to photosystem II. This fast reversible coupling also became visible in the nonphotochemical changes of the fluorescence quantum yield.
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