Evidence map›Paper›PMID 16596412›Full record

ArticlePlanta2006

Posttranslational regulation of pyruvate, orthophosphate dikinase in developing rice (Oryza sativa) seeds.

Chris J Chastain, Jarrod W Heck, Thomas A Colquhoun, Dylan G Voge, Xing-You Gu

Abstract read
PubMed Publisher
In one paragraph

Article in Planta, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
1.4field-weighted citation impact, top 20% 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

30 citing papers in PubMed, 61 citations in OpenAlex.

  1. Article
  2. Asparagine Synthetase GenePlants (Basel, Switzerland) · 2025
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  3. Review
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  5. Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. Review
  11. Article
  12. Plant physiology · 2020
    Article
  13. The Pyruvate-Phosphate Dikinase (CFrontiers in plant science · 2020
    Article
  14. Article
  15. Article
  16. A Novel Mutation ofInternational journal of molecular sciences · 2018
    Article
  17. Article
  18. Functions of maize genes encoding pyruvate phosphate dikinase in developing endosperm.Proceedings of the National Academy of Sciences of the United States of America · 2018
    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

5 authors at 2 institutions in 1 country.

Chris J ChastainDepartment of Biosciences, Minnesota State University-Moorhead, Moorhead, MN 56563, USA. chastain@mnstate.edu
Jarrod W Heck
Thomas A Colquhoun
Dylan G Voge
Xing-You Gu
Minnesota State University Moorhead · USNorth Dakota State University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Pyruvate, orthophosphate dikinase (PPDK; E.C.2.7.9.1) is most well known as a photosynthetic enzyme in C4 plants. The enzyme is also ubiquitous in C3 plant tissues, although a precise non-photosynthetic C3 function(s) is yet to be validated, owing largely to its low abundance in most C3 organs. The single C3 organ type where PPDK is in high abundance, and, therefore, where its function is most amenable to elucidation, are the developing seeds of graminaceous cereals. In this report, we suggest a non-photosynthetic function for C3 PPDK by characterizing its abundance and posttranslational regulation in developing Oryza sativa (rice) seeds. Using primarily an immunoblot-based approach, we show that PPDK is a massively expressed protein during the early syncitial-endosperm/-cellularization stage of seed development. As seed development progresses from this early stage, the enzyme undergoes a rapid, posttranslational down-regulation in activity and amount via regulatory threonyl-phosphorylation (PPDK inactivation) and protein degradation. Immunoblot analysis of separated seed tissue fractions (pericarp, embryo + aleurone, seed embryo) revealed that regulatory phosphorylation of PPDK occurs in the non-green seed embryo and green outer pericarp layer, but not in the endosperm + aleurone layer. The modestly abundant pool of inactive PPDK (phosphorylated + dephosphorylated) that was found to persist in mature rice seeds was shown to remain largely unchanged (inactive) upon seed germination, suggesting that PPDK in rice seeds function in developmental rather than in post-developmental processes. These and related observations lead us to postulate a putative function for the enzyme that aligns its PEP to pyruvate-forming reaction with biosynthetic processes that are specific to early cereal seed development.

Indexed as

Gene Expression Regulation, EnzymologicGene Expression Regulation, PlantGerminationImmunoblottingIsoenzymesMagnoliopsidaOryzaPhosphorylationProtein Processing, Post-TranslationalPyruvate, Orthophosphate DikinaseSeedsIsoenzymesPyruvate, Orthophosphate Dikinase

Identifiers

PMID16596412
OpenAlexW2159862205

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.