Evidence map›Paper›PMID 20018655›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2010

Chloroplast acetyl-CoA carboxylase activity is 2-oxoglutarate-regulated by interaction of PII with the biotin carboxyl carrier subunit.

Ana Belen Feria Bourrellier, Benoit Valot, Alain Guillot, Françoise Ambard-Bretteville, Jean Vidal, Michael Hodges

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 65 papers.

0numbers the graph read from it
0cells of the map it votes in
65citing papers in PubMed
2.7field-weighted citation impact, top 10% 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

65 citing papers in PubMed, 175 citations in OpenAlex.

  1. Review
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  4. Article
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  8. Evolution of the regulatory subunits for the heteromeric acetyl-CoA carboxylase.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2024
    Review
  9. Article
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  13. International journal of molecular sciences · 2021
    Article
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  16. Review
  17. Article
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  20. Review

5 more citing papers are in PubMed but not listed here.

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

6 authors at 3 institutions in 1 country.

Ana Belen Feria BourrellierInstitut de Biotechnologie des Plantes, Centre National de Recherche Scientifique Unité Mixte de Recherche 8618, Université Paris-Sud 11, 91405 Orsay Cedex, France.
Benoit Valot
Alain Guillot
Françoise Ambard-Bretteville
Jean Vidal
Michael Hodges
Université Paris-Sud · FRDépartement Génétique Animale · FRInstitut des Sciences des Plantes de Paris Saclay · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The PII protein is a signal integrator involved in the regulation of nitrogen metabolism in bacteria and plants. Upon sensing of cellular carbon and energy availability, PII conveys the signal by interacting with target proteins, thereby modulating their biological activity. Plant PII is located to plastids; therefore, to identify new PII target proteins, PII-affinity chromatography of soluble extracts from Arabidopsis leaf chloroplasts was performed. Several proteins were retained only when Mg-ATP was present in the binding medium and they were specifically released from the resin by application of a 2-oxoglutarate-containing elution buffer. Mass spectroscopy of SDS/PAGE-resolved protein bands identified the biotin carboxyl carrier protein subunits of the plastidial acetyl-CoA carboxylase (ACCase) and three other proteins containing a similar biotin/lipoyl-binding motif as putative PII targets. ACCase is a key enzyme initiating the synthesis of fatty acids in plastids. In in vitro reconstituted assays supplemented with exogenous ATP, recombinant Arabidopsis PII inhibited chloroplastic ACCase activity, and this was completely reversed in the presence of 2-oxoglutarate, pyruvate, or oxaloacetate. The inhibitory effect was PII-dose-dependent and appeared to be PII-specific because ACCase activity was not altered in the presence of other tested proteins. PII decreased the V(max) of the ACCase reaction without altering the K(m) for acetyl-CoA. These data show that PII function has evolved between bacterial and plant systems to control the carbon metabolism pathway of fatty acid synthesis in plastids.

Indexed as

Acetyl-CoA CarboxylaseAcetyl Coenzyme AArabidopsisArabidopsis ProteinsBiotinChloroplastsKetoglutaric AcidsMolecular Sequence DataPII Nitrogen Regulatory ProteinsPlant LeavesProtein SubunitsRecombinant Fusion ProteinsAcetyl-CoA CarboxylaseAcetyl Coenzyme AArabidopsis ProteinsBiotinKetoglutaric AcidsPII Nitrogen Regulatory ProteinsPII protein, ArabidopsisProtein SubunitsRecombinant Fusion Proteins

Identifiers

PMID20018655
PMCPMC2806706
OpenAlexW2098576269

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.