Evidence map›Paper›PMID 21311031›Full record

ArticlePlant physiology2011

Proteins of diverse function and subcellular location are lysine acetylated in Arabidopsis.

Iris Finkemeier, Miriam Laxa, Laurent Miguet, Andrew J M Howden, Lee J Sweetlove

Open access · hybridAbstract read
In one paragraph

Article in Plant physiology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 128 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
128citing papers in PubMed, 1 pooled it
9.8field-weighted citation impact, top 2% 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

128 citing papers in PubMed, 1 synthesis or guideline pooled it, 256 citations in OpenAlex.

  1. Pooled it
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  15. Comprehensive Proteome and Acetylome Analysis of Needle Senescence inInternational journal of molecular sciences · 2024
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68 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

5 authors at 1 institution in 1 country.

Iris FinkemeierDepartment of Plant Sciences, University of Oxford, Oxford OX1 3RB, United Kingdom.
Miriam Laxa
Laurent Miguet
Andrew J M Howden
Lee J Sweetlove
University of Oxford · GB

Funding

Biotechnology and Biological Sciences Research Council
6 · The paper itself

Abstract

Acetylation of the ε-amino group of lysine (Lys) is a reversible posttranslational modification recently discovered to be widespread, occurring on proteins outside the nucleus, in most subcellular locations in mammalian cells. Almost nothing is known about this modification in plants beyond the well-studied acetylation of histone proteins in the nucleus. Here, we report that Lys acetylation in plants also occurs on organellar and cytosolic proteins. We identified 91 Lys-acetylated sites on 74 proteins of diverse functional classes. Furthermore, our study suggests that Lys acetylation may be an important posttranslational modification in the chloroplast, since four Calvin cycle enzymes were acetylated. The plastid-encoded large subunit of Rubisco stands out because of the large number of acetylated sites occurring at important Lys residues that are involved in Rubisco tertiary structure formation and catalytic function. Using the human recombinant deacetylase sirtuin 3, it was demonstrated that Lys deacetylation significantly affects Rubisco activity as well as the activities of other central metabolic enzymes, such as the Calvin cycle enzyme phosphoglycerate kinase, the glycolytic enzyme glyceraldehyde 3-phosphate dehydrogenase, and the tricarboxylic acid cycle enzyme malate dehydrogenase. Our results demonstrate that Lys acetylation also occurs on proteins outside the nucleus in Arabidopsis (Arabidopsis thaliana) and that Lys acetylation could be important in the regulation of key metabolic enzymes.

Indexed as

Protein Processing, Post-TranslationalAcetylationArabidopsisArabidopsis ProteinsCell NucleusChloroplastsChromatography, LiquidLysineMitochondriaPhotosynthesisProtein Structure, TertiaryProteomeRibulose-Bisphosphate CarboxylaseTandem Mass SpectrometryArabidopsis ProteinsLysineProteomeRibulose-Bisphosphate Carboxylase

Identifiers

PMID21311031
PMCPMC3091095
OpenAlexW2129926698

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.