Evidence map›Paper›PMID 28679357›Full record

ArticleBMC genomics2017

Genome-scale analysis of regulatory protein acetylation enzymes from photosynthetic eukaryotes.

R Glen Uhrig, Pascal Schläpfer, Devang Mehta, Matthias Hirsch-Hoffmann, Wilhelm Gruissem

Open access · goldAbstract read
In one paragraph

Article in BMC genomics, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
0.6field-weighted citation impact, top 34% 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

6 citing papers in PubMed, 12 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Review
  5. Article
  6. Lysine acetylation as drug target in fungi: an underexplored potential in Aspergillus spp.Brazilian journal of microbiology : [publication of the Brazilian Society for Microbiology] · 2020
    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

5 authors at 2 institutions in 3 countries.

R Glen UhrigDepartment of Biology, Institute of Molecular Plant Biology, ETH Zurich, Universitätstrasse 2, 8092, Zurich, Switzerland. ruhrig@ethz.ch.ORCID 0000-0003-2773-4381
Pascal SchläpferDepartment of Biology, Institute of Molecular Plant Biology, ETH Zurich, Universitätstrasse 2, 8092, Zurich, Switzerland.ORCID 0000-0002-0828-8681
Devang MehtaDepartment of Biology, Institute of Molecular Plant Biology, ETH Zurich, Universitätstrasse 2, 8092, Zurich, Switzerland.ORCID 0000-0002-8911-1174
Matthias Hirsch-HoffmannDepartment of Biology, Institute of Molecular Plant Biology, ETH Zurich, Universitätstrasse 2, 8092, Zurich, Switzerland.ORCID 0000-0002-4802-754X
Wilhelm GruissemDepartment of Biology, Institute of Molecular Plant Biology, ETH Zurich, Universitätstrasse 2, 8092, Zurich, Switzerland.
ETH Zurich · CHCarnegie Institution for Science · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundReversible protein acetylation occurring on Lys-N

resultsWe report a genome-scale analysis of lysine acetyltransferase (KAT)- and lysine deacetylase (KDAC)-families from 53 photosynthetic eukaryotes. KAT and KDAC orthologs were identified in sequenced genomes ranging from glaucophytes and algae to land plants and then analyzed for evolutionary relationships. Based on consensus molecular phylogenetic and subcellular localization data we found new sub-classes of enzymes in established KAT- and KDAC-families. Specifically, we identified a non-photosynthetic origin of the HD-tuin family KDACs, a new monocot-specific Class I HDA-family sub-class, and a phylogenetically distinct Class II algal/heterokont sub-class which maintains an ankyrin domain not conserved in land plant Class II KDACs. Protein structure analysis showed that HDA- and SRT-KDACs exist as bare catalytic subunits with highly conserved median protein length, while all KATs maintained auxiliary domains, with CBP- and TAF

conclusionsOur results reveal new evolutionary, structural, and biological insights into the KAT- and KDAC-families of photosynthetic eukaryotes, including evolutionary parallels to protein kinases and protein phosphatases. Further, we provide a comprehensive annotation framework through our extensive phylogenetic analysis, from which future research investigating aspects of protein acetylation in plants can use to position new findings in a broader context.

Indexed as

PhotosynthesisAcetylationAmino Acid SequenceEukaryotaEvolution, MolecularGenomicsLysine AcetyltransferasesPhylogenyPlantsProtein Processing, Post-TranslationalSequence AlignmentTranscription FactorsLysine AcetyltransferasesTranscription FactorsGenomicsLysine AcetyltransferaseLysine DeacetylasePhotosynthetic eukaryotesPost-translational modificationsProtein Acetylation

Identifiers

PMID28679357
PMCPMC5499015
OpenAlexW2732730354

What OpenQuestion holds

Textmetadata
LicenceCC BY
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Registered trials

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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.