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Review
. 2004 Jul;16(7):1650-60.
doi: 10.1105/tpc.160770.

Genetics of the biogenesis and dynamics of the photosynthetic machinery in eukaryotes

Jean-David Rochaix  1
Affiliations
Review

Genetics of the biogenesis and dynamics of the photosynthetic machinery in eukaryotes

Jean-David Rochaix. Plant Cell. 2004 Jul.
No abstract available

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Figures

Figure 1.
Figure 1.
Biosynthesis of the Photosynthetic Apparatus by the Nucleocytosolic and Chloroplast Genetic Systems. The red line refers to nucleus-encoded factors that are required for the different chloroplast posttranscriptional steps. The blue and green lines refer to nucleus and chloroplast-encoded proteins, respectively, that are part of the photosynthetic machinery. Thylakoids are indicated as green vesicles. The four pathways for protein insertion/translocation in the thylakoid membranes are indicated (SRP, Sec, Tat [ΔpH-dependent pathway], and Spn [spontaneous insertions]). 70S, chloroplast ribosomes; 80S, cytosolic ribosomes.
Figure 2.
Figure 2.
CES Model for Assembly of the Cytochrome b6f Complex. The N-terminal lumenal domain (bottom part), the trans-membrane region, and the stromal C-terminal domain of cytochrome f (top part) are indicated. In the fully assembled state, the C-terminal domain of cytochrome f is shielded by the other subunits of the complex. In the unassembled state, this C-terminal end represses the initiation of translation of the petA mRNA of cytochrome f most likely indirectly through a trans-acting factor.
Figure 3.
Figure 3.
NPQ and State Transition. (A) Xanthophyll biosynthetic pathway. The reactions of the xanthophyll cycle are marked with red arrows. The reactions that are affected in the npq1 and npq2 mutants are indicated. (B) Model for NPQ (adapted from Muller et al., 2001). I to IV correspond to the different PSII fluorescence lifetime states. I. In low light (LL), no quenching occurs. II. In high light (HL), protonation of PsbS and other LHC proteins occurs accompanied by a change in the fluorescence lifetime to 1.6 ns. III. Binding of zeaxanthin and protons leads to the formation of a quenching complex with altered conformation detectable as an absorbance change at 535 nm and with a faster 0.4-ns fluorescence lifetime component. IV. Upon a shift from high to low light, deprotonation occurs faster than epoxydation of zeaxanthin to violaxanthin. Fluorescence lifetimes are highlighted. V, violaxanthin; A, antheraxanthin; Z, zeaxanthin. (C) State transitions. In state I, the plastoquinone pool is oxidized, and the mobile part of LHCII (dark green) is associated with PSII. After excitation with 650-nm light that is preferentially absorbed by LHCII, a transition to state II occurs: the plastoquinone pool (PQ) is reduced and activation of the LHCII kinase occurs through the cytochrome b6f complex leading to the phosphorylation of LHCII. The phosphorylated mobile part of LHCII is displaced from PSII and reconnected to PSI. Excitation with 700-nm light preferentially absorbed by LHCI oxidizes the plastoquinone pool, triggering a transition from state II to state I. The LHCII kinase is inactivated, and a phosphatase dephosphorylates LHCII, which moves back to PSII. In Chlamydomonas, a switch from linear to cyclic electron flow occurs upon transition from state I to state II.
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