Characterization of New Strains of Nonphotosynthetic Mutants of Chlamydomonas reinhardtii III. : Photosystem II-Related Thylakoid Proteins in Five Mutants and Double Mutants

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PS II-enriched particles of the wild type, of three mutants and of two double mutants of Chlamydomonas reinhardtii were analyzed by lithium dodecylsulfate polyacrylamide gel electrophoresis at 4℃. The mutant Pg 27 was devoid of light-harvesting Chl-protein complex (CP) CP II, but had normal cytochrome b-559 and displayed all wild type photochemical activities. The mutant Fl 50 lacked a pool of cytochrome b-559 photooxidizable at 77 K but was able to photooxidize a second pool at 293 K in the presence of FCCP; it showed some weak PS II activity. The mutant Fl 39 lacked both these cytochrome 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 Chl b and of CP II. In these four mutants having impaired PS II function, five proteins of M_r=50,000, 47,000, 33,000, 27,000 and 19,000 were totally (Fl 39, Fl 39 Pg 28) or partly (Fl 50, Fl 50 Pg 27) missing. The first two of these proteins corresponded to the apoproteins of CP III and IV. These results pointed out a strong correlation between these five proteins, cytochrome b-559 and PS II primary photochemistry. In mutation and cross experiments, these five PS II-associated proteins and cytochrome b-559 appeared to be linked characters controlled by nuclear gene(s), but they behaved independently of CP II.
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