Assembly of Protein Subunits within the Stromal Ridge of Photosystem I. Structural Changes between Unbound and Sequentially PS I-bound Polypeptides and Correlated Changes of the Magnetic Properties of the Terminal Iron Sulfur Clusters

Antonkine, Mikhail L.; Jordan, Patrick; Fromme, Petra; Krauß, Norbert; Golbeck, John H.; Stehlik, D.

doi:10.1016/s0022-2836(03)00145-1

Cited by 62 publications

(92 citation statements)

References 39 publications

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“…The initial event in PSI assembly involves subunits encoded by the plastome: The formation of the heterodimer PsaA/PsaB is followed by association of PsaC, which is needed for further binding of PsaD and PsaE (Antonkine et al, 2003) and then a number of smaller subunits are added. While PSI in plants can accumulate in the absence of most small subunits, it is well known that mutants devoid of the PsaA/B dimer are unable to assemble a functional PSI core complex, although some peripheral subunits or detached Lhca can accumulate in the thylakoids (Redding et al, 1999;.…”

Section: Comparison Between Nox and Other Mutants Affected In The Biomentioning

confidence: 99%

The Arabidopsis nox Mutant Lacking Carotene Hydroxylase Activity Reveals a Critical Role for Xanthophylls in Photosystem I Biogenesis

et al. 2013

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Carotenes, and their oxygenated derivatives xanthophylls, are essential components of the photosynthetic apparatus. They contribute to the assembly of photosynthetic complexes and participate in light absorption and chloroplast photoprotection. Here, we studied the role of xanthophylls, as distinct from that of carotenes, by characterizing a no xanthophylls (nox) mutant of Arabidopsis thaliana, which was obtained by combining mutations targeting the four carotenoid hydroxylase genes. nox plants retained a-and b-carotenes but were devoid in xanthophylls. The phenotype included depletion of light-harvesting complex (LHC) subunits and impairment of nonphotochemical quenching, two effects consistent with the location of xanthophylls in photosystem II antenna, but also a decreased efficiency of photosynthetic electron transfer, photosensitivity, and lethality in soil. Biochemical analysis revealed that the nox mutant was specifically depleted in photosystem I function due to a severe deficiency in PsaA/B subunits. While the stationary level of psaA/B transcripts showed no major differences between genotypes, the stability of newly synthesized PsaA/B proteins was decreased and translation of psaA/B mRNA was impaired in nox with respect to wild-type plants. We conclude that xanthophylls, besides their role in photoprotection and LHC assembly, are also needed for photosystem I core translation and stability, thus making these compounds indispensable for autotrophic growth.

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Section: Comparison Between Nox and Other Mutants Affected In The Biomentioning

confidence: 99%

The Arabidopsis nox Mutant Lacking Carotene Hydroxylase Activity Reveals a Critical Role for Xanthophylls in Photosystem I Biogenesis

et al. 2013

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“…Upon illumination, the electron emitted from the excited P700 * near the lumenal side of the thylakoid membrane is transferred across the membrane to the [4Fe-4S] clusters of subunit PsaC on the stromal side (Antonkine et al 2003). The [4Fe-4S] clusters in turn reduce the [2Fe-2S] cluster of soluble ferredoxin.…”

Section: Reduced Ferredoxin Is Produced In the Light Reaction Of Photmentioning

confidence: 99%

Structural Basis of Redox Signaling in Photosynthesis: Structure and Function of Ferredoxin:thioredoxin Reductase and Target Enzymes

Dai

Johansson

Miginiac‐Maslow

et al. 2004

Photosynthesis Research

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The role of the ferredoxin:thioredoxin system in the reversible light activation of chloroplast enzymes by thioldisulfide interchange with thioredoxins is now well established. Recent fruitful collaboration between biochemists and structural biologists, reflected by the shared authorship of the paper, allowed to solve the structures of all of the components of the system, including several target enzymes, thus providing a structural basis for the elucidation of the activation mechanism at a molecular level. In the present Review, these structural data are analyzed in conjunction with the information that was obtained previously through biochemical and site-directed mutagenesis approaches. The unique 4Fe-4S cluster enzyme ferredoxin:thioredoxin reductase (FTR) uses photosynthetically reduced ferredoxin as an electron donor to reduce the disulfide bridge of different thioredoxin isoforms. Thioredoxins in turn reduce regulatory disulfides of various target enzymes. This process triggers conformational changes on these enzymes, allowing them to reach optimal activity. No common activation mechanism can be put forward for these enzymes, as every thioredoxin-regulated protein undergoes specific structural modifications. It is thus important to solve the structures of the individual target enzymes in order to fully understand the molecular mechanism of the redox regulation of each of them.Abbreviations: FBPase -fructose-

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“…In the photosynthetic electron transport chains of cyanobacteria and chloroplasts of higher plants, iron-sulfur (Fe/S) 4 clusters not only serve as the terminal electron-accepting cofactors in photosystem (PS) I but they also act as electron transfer cofactors in the cytochrome b 6 f complex and in soluble ferredoxin. PS I is a large, membrane-protein complex that catalyzes the light-induced transfer of electrons from plastocyanin or cytochrome c 6 in the thylakoid lumen to ferredoxin or flavodoxin in the cytoplasm (1,2).…”

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confidence: 99%

“…The PS I electron transport chain consists of P700 (Chl a-Chl aЈ dimer), A 0 (Chl a monomer), A 1 (phylloquinone), and three [4Fe-4S] clusters, which are the terminal electron acceptors denoted F X , F A , and F B . PsaA and PsaB each provide two cysteine (Cys) ligands to the intrasubunit [4Fe-4S] F X cluster, and the F A and F B terminal electron acceptors are bound to a 9-kDa soluble protein, PsaC, which forms a ridge on the stromal surface of PS I with PsaD and PsaE (4). Our previous studies on PS I biogenesis have shown that the insertion of Fe/S clusters is a key step in its post-translational maturation (5,6).…”

mentioning

confidence: 99%

Biogenesis of Iron-Sulfur Clusters in Photosystem I

Zhao

Heinnickel

Krebs

et al. 2008

Journal of Biological Chemistry

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Assembly of Protein Subunits within the Stromal Ridge of Photosystem I. Structural Changes between Unbound and Sequentially PS I-bound Polypeptides and Correlated Changes of the Magnetic Properties of the Terminal Iron Sulfur Clusters

Cited by 62 publications

References 39 publications

The Arabidopsis nox Mutant Lacking Carotene Hydroxylase Activity Reveals a Critical Role for Xanthophylls in Photosystem I Biogenesis

The Arabidopsis nox Mutant Lacking Carotene Hydroxylase Activity Reveals a Critical Role for Xanthophylls in Photosystem I Biogenesis

Structural Basis of Redox Signaling in Photosynthesis: Structure and Function of Ferredoxin:thioredoxin Reductase and Target Enzymes

Biogenesis of Iron-Sulfur Clusters in Photosystem I

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