Evidence map›Paper›PMID 23192387›Full record

ReviewPlanta2013

From cyanobacteria to plants: conservation of PII functions during plastid evolution.

Vasuki Ranjani Chellamuthu, Vikram Alva, Karl Forchhammer

Open access · bronzeAbstract readReview
PubMed Publisher
In one paragraph

Review in Planta, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
3.1field-weighted citation impact, top 8% 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

29 citing papers in PubMed, 66 citations in OpenAlex.

  1. Ability ofMicroorganisms · 2026
    Article
  2. Article
  3. International journal of molecular sciences · 2026
    Article
  4. Review
  5. Review
  6. Article
  7. N-Acetyl-L-glutamate Kinase ofInternational journal of molecular sciences · 2023
    Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. Review
  14. Article
  15. Review
  16. The Signal Transduction Protein PFrontiers in microbiology · 2019
    Article
  17. Article
  18. Article
  19. Article
  20. Article
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

3 authors at 2 institutions in 1 country.

Vasuki Ranjani ChellamuthuDepartment of Protein Evolution, Max Planck Institute for Developmental Biology, Spemannstrasse 35, Tübingen, Germany. vasuki-ranjani.chellamuthu@tuebingen.mpg.de
Vikram Alva
Karl Forchhammer
University of Tübingen · DEMax Planck Society · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

This article reviews the current state-of-the-art concerning the functions of the signal processing protein PII in cyanobacteria and plants, with a special focus on evolutionary aspects. We start out with a general introduction to PII proteins, their distribution, and their evolution. We also discuss PII-like proteins and domains, in particular, the similarity between ATP-phosphoribosyltransferase (ATP-PRT) and its PII-like domain and the complex between N-acetyl-L-glutamate kinase (NAGK) and its PII activator protein from oxygenic phototrophs. The structural basis of the function of PII as an ATP/ADP/2-oxoglutarate signal processor is described for Synechococcus elongatus PII. In both cyanobacteria and plants, a major target of PII regulation is NAGK, which catalyzes the committed step of arginine biosynthesis. The common principles of NAGK regulation by PII are outlined. Based on the observation that PII proteins from cyanobacteria and plants can functionally replace each other, the hypothesis that PII-dependent NAGK control was under selective pressure during the evolution of plastids of Chloroplastida and Rhodophyta is tested by bioinformatics approaches. It is noteworthy that two lineages of heterokont algae, diatoms and brown algae, also possess NAGK, albeit lacking PII; their NAGK however appears to have descended from an alphaproteobacterium and not from a cyanobacterium as in plants. We end this article by coming to the conclusion that during the evolution of plastids, PII lost its function in coordinating gene expression through the PipX-NtcA network but preserved its role in nitrogen (arginine) storage metabolism, and subsequently took over the fine-tuned regulation of carbon (fatty acid) storage metabolism, which is important in certain developmental stages of plants.

Indexed as

Biological EvolutionAmino Acid SequenceArginineKetoglutaric AcidsMolecular Sequence DataPhosphotransferases (Alcohol Group Acceptor)Photosystem II Protein ComplexPhylogenyPlantsPlastidsProtein Interaction MappingSignal TransductionStructure-Activity RelationshipSynechococcusArginineKetoglutaric AcidsN-acetylglucosamine kinasePhosphotransferases (Alcohol Group Acceptor)Photosystem II Protein Complex

Identifiers

PMID23192387
OpenAlexW2025257124

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.