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THE PLANT CELL, Vol 7, Issue 6 689-704, Copyright © 1995 by American Society of Plant Biologists
Light-Harvesting Chlorophyll a/b Complexes: Interdependent Pigment Synthesis and Protein Assembly
G. F. Plumley and G. W. Schmidt
Institute of Marine Science, University of Alaska, Fairbanks, Alaska 99775
The biogenetic interdependence of light-harvesting chlorophyll (Chl) a/b
proteins (LHCPs) and antenna pigments has been analyzed for two nuclear
mutants of Chlamydomonas that have low levels of Chl b, neoxanthin, and
loroxanthin. In mutant PA2.1, the apoprotein precursors (pLHCP II) of the
major light-harvesting complex LHC II were synthesized at approximately
wild-type rates, processed to their mature size, and rapidly degraded.
Because the bulk of labile LHCP II in PA2.1 was soluble, a thylakoid
integration factor apparently is defective in this strain. Chl a, Chl b,
neoxanthin, and loroxanthin synthesis and accumulation were coordinately
reduced in PA2.1, indicating that LHCP II play important regulatory or
substrate roles in de novo synthesis of these pigments. Mutant GE2.27 is
impaired principally in Chl b synthesis but nonetheless accumulated
wild-type levels of all LHCPs. Topology studies of the GE2.27 LHCP II
demonstrated that their insertion into thylakoids was incomplete even
though they were not structurally altered. Thus, Chl b formation mediates
conformational changes of LHCP II after thylakoid integration is initiated.
GE2.27 also exhibited very low rates of neoxanthin synthesis and was unable
to accumulate loroxanthin. Revertant GE2.27 strains with varying capacities
for Chl b formation provided additional evidence that neoxanthin synthesis
and accumulation are coupled with the final steps of LHCP II integration
into thylakoids. We propose that biogenesis of LHC includes interdependent
pigment synthesis/assembly events that occur during LHCP integration into
the thylakoid membrane and that defects in these events account for the
pleiotropic characteristics of many Chl b-deficient mutants.
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