Evidence map›Paper›PMID 22786888›Full record

ArticlePlant physiology2012

Synergistic interactions between carotene ring hydroxylases drive lutein formation in plant carotenoid biosynthesis.

Rena F Quinlan, Maria Shumskaya, Louis M T Bradbury, Jesús Beltrán, Chunhui Ma, Edward J Kennelly, Eleanore T Wurtzel

Open access · hybridAbstract read
In one paragraph

Article in Plant physiology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.

0numbers the graph read from it
0cells of the map it votes in
44citing papers in PubMed
3.2field-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

44 citing papers in PubMed, 104 citations in OpenAlex.

  1. Trial
  2. Article
  3. Review
  4. Article
  5. Cytochromes P450 evolution in the plant terrestrialization context.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2024
    Review
  6. Article
  7. CitrusHorticulture research · 2023
    Article
  8. Article
  9. Article
  10. Overexpression ofFrontiers in plant science · 2022
    Article
  11. Article
  12. Review
  13. Article
  14. Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. Structural basis for plant lutein biosynthesis from α-carotene.Proceedings of the National Academy of Sciences of the United States of America · 2020
    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

7 authors at 2 institutions in 1 country.

Rena F QuinlanDepartment of Biological Sciences, Lehman College, City University of New York, Bronx, New York 10468, USA.
Maria Shumskaya
Louis M T Bradbury
Jesús Beltrán
Chunhui Ma
Edward J Kennelly
Eleanore T Wurtzel
Lehman College · USCity University of New York · US

Funding

REGULATION OF PROVITAMIN A CAROTENOID BIOSYNTHESIS IN MAIZESC1GM081160 · NIGMS · HERBERT H. LEHMAN COLLEGE · PI WURTZEL, ELEANORE T · 2007 to 2010
$1.7M
Plant Polyphenols for the Treatment of Chronic Obstructive Pulmonary DiseaseSC1HL096016 · NHLBI · HERBERT H. LEHMAN COLLEGE · PI KENNELLY, EDWARD JAMES · 2008 to 2011
$1.1M
NHLBI NIH HHS 5SC1HL096016NIGMS NIH HHS GM081160NIGMS NIH HHS SC1 GM081160
6 · The paper itself

Abstract

Plant carotenoids play essential roles in photosynthesis, photoprotection, and as precursors to apocarotenoids. The plastid-localized carotenoid biosynthetic pathway is mediated by well-defined nucleus-encoded enzymes. However, there is a major gap in understanding the nature of protein interactions and pathway complexes needed to mediate carotenogenesis. In this study, we focused on carotene ring hydroxylation, which is performed by two structurally distinct classes of enzymes, the P450 CYP97A and CYP97C hydroxylases and the nonheme diiron HYD enzymes. The CYP97A and HYD enzymes both function in the hydroxylation of β-rings in carotenes, but we show that they are not functionally interchangeable. The formation of lutein, which involves hydroxylation of both β- and ε-rings, was shown to require the coexpression of CYP97A and CYP97C enzymes. These enzymes were also demonstrated to interact in vivo and in vitro, as determined using bimolecular fluorescence complementation and a pull-down assay, respectively. We discuss the role of specific hydroxylase enzyme interactions in promoting pathway flux and preventing the formation of pathway dead ends. These findings will facilitate efforts to manipulate carotenoid content and composition for improving plant adaptation to climate change and/or for enhancing nutritionally important carotenoids in food crops.

Indexed as

Base SequenceCarotenoidsChlorophyllChloroplast ProteinsCytochrome P-450 Enzyme SystemEscherichia coliGene Expression Regulation, EnzymologicGene Expression Regulation, PlantGenetic Complementation TestHydroxylationLuteinMixed Function OxygenasesMolecular Sequence DataOryzaPisum sativumPlastidsCarotenoidsChlorophyllChloroplast ProteinsCytochrome P-450 Enzyme SystemLuteinMixed Function Oxygenases

Identifiers

PMID22786888
PMCPMC3440199
OpenAlexW1990598606

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.