Evidence map›Paper›PMID 12897255›Full record

ArticleThe Plant cell2003

Cytoplasmic N-terminal protein acetylation is required for efficient photosynthesis in Arabidopsis.

Paolo Pesaresi, Nora A Gardner, Simona Masiero, Angela Dietzmann, Lutz Eichacker, Reed Wickner, Francesco Salamini, Dario Leister

Open access · bronzeAbstract readComparative Study
In one paragraph

Article in The Plant cell, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 54 papers.

0numbers the graph read from it
0cells of the map it votes in
54citing papers in PubMed
2.3field-weighted citation impact, top 12% 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

54 citing papers in PubMed, 120 citations in OpenAlex.

  1. Science advances · 2025
    Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Review
  7. HYPK promotes the activity of theScience advances · 2022
    Article
  8. Review
  9. Review
  10. Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. NAA50 Is an Enzymatically ActivePlant physiology · 2020
    Article
  16. Article
  17. Article
  18. Article
  19. Review
  20. Review
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

8 authors at 3 institutions in 2 countries.

Paolo PesaresiAbteilung für Pflanzenzüchtung und Ertragsphysiologie, Max-Planck-Institut für Züchtungsforschung, D-50829 Köln, Germany.
Nora A Gardner
Simona Masiero
Angela Dietzmann
Lutz Eichacker
Reed Wickner
Francesco Salamini
Dario Leister
Max Planck Society · DENational Institute of Diabetes and Digestive and Kidney Diseases · USLudwig-Maximilians-Universität München · DE

Funding

YEAST RNA VIROLOGYZ01DK024940 · NIDDK · NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES · PI WICKNER, REED B. · 1986 to 2008
$64k
6 · The paper itself

Abstract

The Arabidopsis atmak3-1 mutant was identified on the basis of a decreased effective quantum yield of photosystem II. In atmak3-1, the synthesis of the plastome-encoded photosystem II core proteins D1 and CP47 is affected, resulting in a decrease in the abundance of thylakoid multiprotein complexes. DNA array-based mRNA analysis indicated that extraplastid functions also are altered. The mutation responsible was localized to AtMAK3, which encodes a homolog of the yeast protein Mak3p. In yeast, Mak3p, together with Mak10p and Mak31p, forms the N-terminal acetyltransferase complex C (NatC). The cytoplasmic AtMAK3 protein can functionally replace Mak3p, Mak10p, and Mak31p in acetylating N termini of endogenous proteins and the L-A virus Gag protein. This result, together with the finding that knockout of the Arabidopsis MAK10 homolog does not result in obvious physiological effects, indicates that AtMAK3 function does not require NatC complex formation, as it does in yeast. We suggest that N-acetylation of certain chloroplast precursor protein(s) is necessary for the efficient accumulation of the mature protein(s) in chloroplasts.

Indexed as

PhotosynthesisAcetylationAmino Acid SequenceArabidopsisArabidopsis ProteinsArylamine N-AcetyltransferaseBase SequenceCell NucleusCytoplasmDNA, PlantGenes, PlantGenetic Complementation TestMacromolecular SubstancesMitochondriaMolecular Sequence DataMultiprotein ComplexesArabidopsis ProteinsArylamine N-AcetyltransferaseDNA, PlantMacromolecular SubstancesMultiprotein ComplexesSaccharomyces cerevisiae Proteins

Identifiers

PMID12897255
PMCPMC167172
OpenAlexW2143348980

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.