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Chloroplast Proteins Related to Photosystem II in Chlamydomonas Reinhardtii: Mutants and Trypsin-Treated Chloroplast Particles

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Advances in Photosynthesis Research

Part of the book series: Advances in Agricultural Biotechnology ((AABI,volume 3))

Abstract

Five mutants and double mutants of Chlamydomonas reinhardtii had been isolated and characterized in our laboratory. The mutant Pg 27 was devoid of the light-harvesting chlorophyll-protein complex CP II, but had normal Cyt b-559 and displayed all wild type photochemical activities. The mutant Fl 50 lacked a pool of Cyt b-559 photooxidizable at 77 K but was able to photooxidize a second pool at 293 K in the presence of ADRY agents; it showed some weak PS II activity. The mutant Fl 39 lacked both these Cyt b-559 pools and did not display any PS II activity. The double mutants Fl 39 Pg 28 and Fl 50 Pg 27 had defects similar to those of their respective parents Fl 39 or Fl 50 but, in addition, they were devoid of CP II (Garnier et al. 1979; Maroc, Garnier 1979, 1981; Picaud et al. 1981; Maroc et al. 1983). Table 1 indicates some main characteristics of these mutants.

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Abbreviations

ADRY:

acceleration of the deactivation reactions of the water-splitting enzyme system Y of photosynthesis

Chl:

chlorophyll

CP:

chlorophyll-protein complex

Cyt b-559:

cytochrome b-559

DCIP:

2,6-dichlorophenolindophenol

DCMU:

3-(3,4-dichlorophenyl)-1, 1-dimethylurea

DPC:

diphenylcarbazide

Mr:

relative molecular mass

PS:

photosystem

References

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Garnier, J., Maroc, J. (1984). Chloroplast Proteins Related to Photosystem II in Chlamydomonas Reinhardtii: Mutants and Trypsin-Treated Chloroplast Particles. In: Sybesma, C. (eds) Advances in Photosynthesis Research. Advances in Agricultural Biotechnology, vol 3. Springer, Dordrecht. https://doi.org/10.1007/978-94-017-4973-2_40

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  • DOI: https://doi.org/10.1007/978-94-017-4973-2_40

  • Publisher Name: Springer, Dordrecht

  • Print ISBN: 978-90-247-2944-9

  • Online ISBN: 978-94-017-4973-2

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