Evidence map›Paper›PMID 22328157›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2012

Thioredoxin-insensitive plastid ATP synthase that performs moonlighting functions.

Kaori Kohzuma, Cristina Dal Bosco, Atsuko Kanazawa, Amit Dhingra, Wolfgang Nitschke, Jörg Meurer, David M Kramer

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.5field-weighted citation impact, top 18% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

18 citing papers in PubMed, 47 citations in OpenAlex.

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  4. The chloroplast ATP synthase redox domain inProceedings of the National Academy of Sciences of the United States of America · 2024
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

7 authors at 5 institutions in 3 countries.

Kaori KohzumaPlant Research Laboratory, S222 Plant Biology Building, Michigan State University, East Lansing, MI 48824-1312, USA.
Cristina Dal Bosco
Atsuko Kanazawa
Amit Dhingra
Wolfgang Nitschke
Jörg Meurer
David M Kramer
Michigan State University · USWashington State University · USBioénergétique et Ingénierie des Protéines · FRLudwig-Maximilians-Universität München · DEUniversity of Freiburg · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The chloroplast ATP synthase catalyzes the light-driven synthesis of ATP and acts as a key feedback regulatory component of photosynthesis. Arabidopsis possesses two homologues of the regulatory γ subunit of the ATP synthase, encoded by the ATPC1 and ATPC2 genes. Using a series of mutants, we show that both these subunits can support photosynthetic ATP synthesis in vivo with similar specific activities, but that in wild-type plants, only γ(1) is involved in ATP synthesis in photosynthesis. The γ(1)-containing ATP synthase shows classical light-induced redox regulation, whereas the mutant expressing only γ(2)-ATP synthase (gamma exchange-revised ATP synthase, gamera) shows equally high ATP synthase activity in the light and dark. In situ redox titrations demonstrate that the regulatory thiol groups on γ(2)-ATP synthase remain reduced under physiological conditions but can be oxidized by the strong oxidant diamide, implying that the redox potential for the thiol/disulphide transition in γ(2) is substantially higher than that for γ(1). This regulatory difference may be attributed to alterations in the residues near the redox-active thiols. We propose that γ(2)-ATP synthase functions to catalyze ATP hydrolysis-driven proton translocation in nonphotosynthetic plastids, maintaining a sufficient transthylakoid proton gradient to drive protein translocation or other processes. Consistent with this interpretation, ATPC2 is predominantly expressed in the root, whereas modifying its expression results in alteration of root hair development. Phylogenetic analysis suggests that γ(2) originated from ancient gene duplication, resulting in divergent evolution of functionally distinct ATP synthase complexes in dicots and mosses.

Indexed as

Adenosine TriphosphateAmino AcidsAmino Acid SequenceArabidopsisArabidopsis ProteinsBiological Transport, ActiveChloroplast Proton-Translocating ATPasesChloroplastsDiamideEvolution, MolecularGene DuplicationLightMolecular Sequence DataMorphogenesisOxidantsOxidation-ReductionAdenosine TriphosphateAmino AcidsArabidopsis ProteinsChloroplast Proton-Translocating ATPasesDiamideOxidantsThioredoxins

Identifiers

PMID22328157
PMCPMC3295299
OpenAlexW2146277472

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.