The Chloroplast ATP Synthase Features the Characteristic Redox Regulation Machinery

Hisabori, Toru; Sunamura, Ei-Ichiro; Kim, Yusung; Konno, Haruyoshi

doi:10.1089/ars.2012.5044

Cited by 75 publications

(54 citation statements)

References 81 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The chloroplast homologue contains a novel regulatory domain, in which two redox-active cysteine residues are sandwiched between the long ␣ helixes (7). It is now well established that these cysteine residues are reduced to free thiols by thioredoxin in the light and reoxidized in the dark, regulating the activity of the ATP synthase (for review, see Refs 19,31). We found that mutating residues, Asp 211 , Glu 212 , and Glu 226 to Val, Leu, and Leu, respectively, eliminated the classical light-dark regulation of the ATP synthase (Fig.…”

Section: Atp Synthase In Mothra Is Equally Active In the Light-andmentioning

confidence: 62%

“…1, B-D. These residues are in the loop containing the regulatory cysteine residues, a region that is apparently quite flexible and can accommodate large changes (point mutations and deletions) albeit with altered regulatory and catalytic behaviors (18,19,31).…”

Section: Effects Of Altering Three Highly Conserved Acidic Residues Inmentioning

confidence: 99%

“…In another Arabidopsis mutant, cfq (18,35), a single substitution of another highly conserved glutamate group (E244K) in the ␥ subunit resulted in more negative redox potential, rendering the complex more prone to oxidation in the dark. Deletion or mutation of the negatively charged residues Glu 210 -Asp 211 -Glu 212 in this region in the thermophilic bacterium Bacillus PS3 (30,31,36) resulted in reverse redox sensitivity, i.e. becoming more active in the oxidized form and less in the reduced.…”

Section: Atp Synthase In Mothra Is Equally Active In the Light-andmentioning

confidence: 99%

See 2 more Smart Citations

Light- and Metabolism-related Regulation of the Chloroplast ATP Synthase Has Distinct Mechanisms and Functions

Kohzuma

Bosco

Meurer

et al. 2013

Journal of Biological Chemistry

View full text Add to dashboard Cite

Background: Chloroplast ATP synthase activity is regulated by both light and metabolic factors, but the relationship between these regulatory modes is not established. Results: Mutating three highly conserved acidic amino acid residues in the ␥ subunit alters light-but not metabolism-induced regulation. Conclusion: Metabolism and light regulation operates via distinct mechanisms. Significance: The chloroplast ATP synthase is a key control point for the light and dark reactions of photosynthesis.

show abstract

Section: Atp Synthase In Mothra Is Equally Active In the Light-andmentioning

confidence: 62%

Section: Effects Of Altering Three Highly Conserved Acidic Residues Inmentioning

confidence: 99%

Section: Atp Synthase In Mothra Is Equally Active In the Light-andmentioning

confidence: 99%

See 1 more Smart Citation

Light- and Metabolism-related Regulation of the Chloroplast ATP Synthase Has Distinct Mechanisms and Functions

Kohzuma

Bosco

Meurer

et al. 2013

Journal of Biological Chemistry

View full text Add to dashboard Cite

show abstract

“…Several mechanisms for the regulation of ATP synthase activity in chloroplasts have been elucidated [37]. Binding of ADP-Mg to the catalytic site strongly inhibits ATP hydrolysis [38].…”

Section: Regulation Of H + Conductivity Via Atp Synthase In the Pgr5 mentioning

confidence: 99%

“…Chloroplast ATP synthase is a thiol enzyme, the activity of which is regulated via a disulfide bond present in the CF 1 γ subunit [37]. To activate ATPase in the light, the disulfide bond is reduced by thioredoxin-f, which is in turn reduced by ferredoxin-thioredoxin reductase.…”

Section: Regulation Of H + Conductivity Via Atp Synthase In the Pgr5 mentioning

confidence: 99%

Role of cyclic electron transport around photosystem I in regulating proton motive force

Wang

Yamamoto

Shikanai

2015

Biochimica et Biophysica Acta (BBA) - Bioenergetics

127

View full text Add to dashboard Cite

In addition to ∆pH formed across the thylakoid membrane, membrane potential contributes to proton motive force (pmf) in chloroplasts. However, the regulation of photosynthetic electron transport is mediated solely by ∆pH. To assess the contribution of two cyclic electron transport pathways around photosystem I (one depending on PGR5/PGRL1 and one on NDH) to pmf formation, electrochromic shift (ECS) was analyzed in the Arabidopsis pgr5 mutant, NDH-defective mutants (ndhs and crr4-2), and their double mutants (ndhs pgr5 and crr4-2 pgr5). In pgr5, the size of the pmf, as represented by ECSt, was reduced by 30% to 47% compared with that in the wild type (WT). A gH+ parameter, which is considered to represent the activity of ATP synthase, was enhanced at high light intensities. However, gH+ recovered to its low-light levels after 20 min in the dark, implying that the elevation in gH+ is due to the disturbed regulation of ATP synthase rather than to photodamage. After long dark adaptation more than 2 h, gH+ was higher in pgr5 than in the WT. During induction of photosynthesis, gH+ was more rapidly elevated in pgr5 than that in the WT. Both results suggest that ATP synthase is not fully inactivated in the dark in pgr5. In the NDH-deficient mutants, ECSt was slightly but significantly lower than in the WT, whereas gH+ was not affected. In the double mutants, ECSt was even lower than in pgr5. These results suggest that both PGR5/PGRL1- and NDH-dependent pathways contribute to pmf formation, although to different extents. This article is part of a Special Issue entitled: Chloroplast Biogenesis.

show abstract

The plastomes of Hyalomonas oviformis and Hyalogonium fusiforme evolved dissimilar architectures after the loss of photosynthesis

et al. 2022

View full text Add to dashboard Cite

The loss of photosynthesis in land plants and algae is typically associated with parasitism but can also occur in free‐living species, including chlamydomonadalean green algae. The plastid genomes (ptDNAs) of colorless chlamydomonadaleans are surprisingly diverse in architecture, including highly expanded forms (Polytoma uvella and Leontynka pallida) as well as outright genome loss (Polytomella species). Here, we explore the ptDNAs of Hyalomonas (Hm.) oviformis (SAG 62‐27; formerly known as Polytoma oviforme) and Hyalogonium (Hg.) fusiforme (SAG 62‐1c), each representing independent losses of photosynthesis within the Chlamydophyceae. The Hm. oviformis ptDNA is moderately sized (132 kb) with a reduced gene complement (but still encoding the ATPase subunits) and is in fact smaller than that of its photosynthetic relative Hyalomonas chlamydogama SAG 11‐48b (198.3 kb). The Hg. fusiforme plastome, however, is the largest yet observed in nonphotosynthetic plants or algae (~463 kb) and has a coding repertoire that is almost identical to that of its photosynthetic relatives in the genus Chlorogonium. Furthermore, the ptDNA of Hg. fusiforme shows no clear evidence of pseudogenization, which is consistent with our analyses showing that Hg. fusiforme is the nonphotosynthetic lineage of most recent origin among known colorless Chlamydophyceae. Together, these new ptDNAs clearly show that, in contrast to parasitic algae, plastid genome compaction is not an obligatory route following the loss of photosynthesis in free‐living algae, and that certain chlamydomonadalean algae have a remarkable propensity for genomic expansion, which can persist regardless of the trophic strategy.

show abstract

The Chloroplast ATP Synthase Features the Characteristic Redox Regulation Machinery

Abstract: The molecular architecture of the chloroplast ATP synthase, which confers redox regulatory properties requires further investigation, in light of the molecular structure of the enzyme complex as well as the physiological significance of the regulation system.

Cited by 75 publications

References 81 publications

Light- and Metabolism-related Regulation of the Chloroplast ATP Synthase Has Distinct Mechanisms and Functions

Light- and Metabolism-related Regulation of the Chloroplast ATP Synthase Has Distinct Mechanisms and Functions

Role of cyclic electron transport around photosystem I in regulating proton motive force

The plastomes of Hyalomonas oviformis and Hyalogonium fusiforme evolved dissimilar architectures after the loss of photosynthesis

Contact Info

Product

Resources

About