Regulation of chlorophyll apoprotein expression and accumulation. Requirements for carotenoids and chlorophyll.

Herrin, David L.; Battey, James F.; Greer, Karen L.; Schmidt, Gregory W.

doi:10.1016/s0021-9258(18)42436-2

Cited by 92 publications

(10 citation statements)

References 39 publications

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“…Incorporation of Chi into the protein complex is thought to occur cotranslationally. Therefore, in the absence of Chi, apoproteins may not accumulate due to a block in translation or rapid degradation of the newly synthesized protein (Klein & Mullet, 1986;Herrin et al, 1992). Recent analysis of Chi a-binding protein synthesis in etioplasts has produced results that favor destabilization and rapid degradation of the apoprotein rather than any impairment in translational initiation and elongation (Kim et al, 1994).…”

Section: Discussionmentioning

confidence: 99%

“…The immobilized polypeptides were incubated with antisera against PsaA/B (a gift from Dr. A. Melis). For immunodecoration, a goat-anti-rabbit IgG-horseradish peroxidase was used followed by color development according to procedures supplied by Bio-Rad. Nondenaturing (green) gel electrophoresis was performed following published procedures (Delepelaire & Chua, 1979;Herrin et al, 1992). Thylakoid membranes were solubilized in LDS sample buffer at 4 °C and size-fractionated through 10% acrylamide gels in the absence of SDS at 4 °C.…”

Section: Methodsmentioning

confidence: 99%

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Site-Directed Mutagenesis of Conserved Histidines in the Helix VIII Domain of PsaB Impairs Assembly of the Photosystem I Reaction Center without Altering Spectroscopic Characteristics of P700

Cui¹,

Bingham²,

Kühn³

et al. 1995

Biochemistry

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The chloroplast psaB gene encodes one of the polypeptides of the photosystem I reaction center heterodimer that coordinates the electron transfer components P700, A0, and A1. Histidine residues in the most highly conserved region of the PsaB protein are predicted to coordinate the P700 reaction center chlorophyll(s) and the initial electron acceptor, A0. Oligonucleotide-mediated site-directed mutagenesis and chloroplast transformation of Chlamydomonas reinhardtii have been used to determine the importance of these conserved histidines in photosystem I reaction center biogenesis and function. It is demonstrated that these histidine residues are essential for stable accumulation of the photosystem I reaction center. Protein pulse-labeling shows that changing the histidine residues impairs a post-translational step in reaction center assembly. Photosystem I complexes from the mutants have been characterized by Electron Nuclear Double Resonance and Electron Spin Echo Envelope Modulation spectroscopy to determine the impact of any mutations on P700+. In all cases we determine that spectroscopic characteristics of P700+ remain unchanged. The implications of these results to current models of the photosystem I reaction center and related bacterial reaction centers are discussed.

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Section: Discussionmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

Site-Directed Mutagenesis of Conserved Histidines in the Helix VIII Domain of PsaB Impairs Assembly of the Photosystem I Reaction Center without Altering Spectroscopic Characteristics of P700

Cui¹,

Bingham²,

Kühn³

et al. 1995

Biochemistry

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“…De novo production of Chl by ChlG is essential for the stable accumulation of Chl-binding apoproteins such as P700, CP47, CP43 and D2 [53,54,150–158], without which photomorphogenesis is delayed [40]. Although the accumulation of Chl and Chl-binding proteins are positively correlated [153,159–162], it is likely that the binding of Chl to these apoproteins is required for their stability and that the onset of Chl biosynthesis does not promote translation of Chl-binding photosystem subunits [54,154,155,163–165]. Furthermore, the binding of Chl to apoproteins appears to specifically require that Chl originates from de novo synthesis by ChlG; addition of Chlide and PPP to a ChlG-containing etioplast fraction resulted in accumulation of P700, CP47, CP43 and D2, whereas direct addition of Chl did not ([51]; L. Eichacker 2022, personal communication).…”

Section: The Role Of Chlorophyll Synthase In Coordination Of Chloroph...mentioning

confidence: 99%

“…As such, a mismatch in the rate of Chl biosynthesis and the synthesis of Chl-binding proteins could result in an excess of free Chl to the detriment of the cell [149]. De novo production of Chl by ChlG is essential for the stable accumulation of Chl-binding apoproteins such as P700, CP47, CP43 and D2 [53,54,[150][151][152][153][154][155][156][157][158], without which photomorphogenesis is delayed [40]. Although the accumulation of Chl and Chl-binding royalsocietypublishing.org/journal/rsos R. Soc.…”

Section: At-chlgmentioning

confidence: 99%

The terminal enzymes of (bacterio)chlorophyll biosynthesis

et al. 2022

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(Bacterio)chlorophylls are modified tetrapyrroles that are used by phototrophic organisms to harvest solar energy, powering the metabolic processes that sustain most of the life on Earth. Biosynthesis of these pigments involves enzymatic modification of the side chains and oxidation state of a porphyrin precursor, modifications that differ by species and alter the absorption properties of the pigments. (Bacterio)chlorophylls are coordinated by proteins that form macromolecular assemblies to absorb light and transfer excitation energy to a special pair of redox-active (bacterio)chlorophyll molecules in the photosynthetic reaction centre. Assembly of these pigment–protein complexes is aided by an isoprenoid moiety esterified to the (bacterio)chlorin macrocycle, which anchors and stabilizes the pigments within their protein scaffolds. The reduction of the isoprenoid ‘tail’ and its addition to the macrocycle are the final stages in (bacterio)chlorophyll biosynthesis and are catalysed by two enzymes, geranylgeranyl reductase and (bacterio)chlorophyll synthase. These enzymes work in conjunction with photosynthetic complex assembly factors and the membrane biogenesis machinery to synchronize delivery of the pigments to the proteins that coordinate them. In this review, we summarize current understanding of the catalytic mechanism, substrate recognition and regulation of these crucial enzymes and their involvement in thylakoid biogenesis and photosystem repair in oxygenic phototrophs.

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“…In higher plants, by regulating chlorophyll synthesis, light also controls the synthesis and accumulation of the D1 protein as well as other chlorophyll binding proteins ( − ). Complete translational elongation and accumulation of the D1 protein depend on chlorophyll binding, stabilizing the D1 synthesis intermediates ( − ).…”

mentioning

confidence: 99%

Recovery of Photosystem II Activity in PhotoinhibitedSynechocystisCells: Light-Dependent Translation Activity Is Required besides Light-Independent Synthesis of the D1 Protein

et al. 2000

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Irreversible photoinactivation of photosystem II (PSII) results in the degradation of the reaction center II D1 protein. In Synechocystis PCC 6714 cells, recovery of PSII activity requires illumination. The rates of photoinactivation and recovery of PSII activity in the light are similar in cells grown in minimal (MM) or glucose-containing medium (GM). Reassembly of PSII with newly synthesized proteins requires degradation of the D1 protein of the photoinactivated PSII. This process may occur in darkness in both types of cells. The degraded D1 protein is, however, only partially replaced by newly synthesized protein in MM cells in darkness while a high level of D1 protein synthesis occurs in darkness in the GM cells. The newly synthesized D1 protein in darkness appears to be assembled with other PSII proteins. However, PSII activity is not recovered in such cells. Illumination of the cells in absence but not in the presence of protein synthesis inhibitors allows recovery of PSII activity.

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Regulation of chlorophyll apoprotein expression and accumulation. Requirements for carotenoids and chlorophyll.

Cited by 92 publications

References 39 publications

Site-Directed Mutagenesis of Conserved Histidines in the Helix VIII Domain of PsaB Impairs Assembly of the Photosystem I Reaction Center without Altering Spectroscopic Characteristics of P700

Site-Directed Mutagenesis of Conserved Histidines in the Helix VIII Domain of PsaB Impairs Assembly of the Photosystem I Reaction Center without Altering Spectroscopic Characteristics of P700

The terminal enzymes of (bacterio)chlorophyll biosynthesis

Recovery of Photosystem II Activity in PhotoinhibitedSynechocystisCells: Light-Dependent Translation Activity Is Required besides Light-Independent Synthesis of the D1 Protein

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