Pigment protein complexes and functional properties of tetratype resulting from crosses between CP1 and CP 2 less Chlamydomonas mutants.

A chlorophyll b-less mutant of Chlamydomonas reinhardtii (Pg 27) was isolated after UV irradiation of the wild type cells. This photosynthetically competent mutant totally lacks chlorophyll b and the CP2 chlorophyll-protein complex. However, SDS-PAGE, proteolytic digestions and immunodetections demonstrated that the 24-25 Kd apoproteins of the lacking CP2 complex are still present in thylakoids of the Pg27 mutant. It is concluded that this CP2-less mutant is affected in the biosynthesis pathway of chlorophyll b.This CP2-less mutant was crossed with a CP1-less mutant (Fl5) Fluorescence emission spectra and fluorescence inductions in the presence of DCMU were analysed in the resulting (cp 2 (-) , cp 1 (+) ), (cp 2 (+) , cp 1 (-) ), (cp 2 (+) , cp 1 (+) ), cp 2 (-) , cp 1 (-) )tetratype. Differences in PS 2 optical cross section and in the relative amplitude or localisation of fluorescence emission peaks fit well with a quadripartite model where PS1 and PS2 would each correspond to a reaction centre core complex (CP1 and CP2 respectively) associated to a light harvesting antenna (LHC1 and LHC2 respectively). The occurrence of energy transfers from PS1 peripheral antenna to PS2 in the Fl 5 mutant shows that, in absence of CP1, at least a part of its associated PS1 light harvesting antenna migrates in the PS2 containing appressed thylakoids.