Evidence map›Paper›PMID 23336284›Full record

ArticleBMC genomics2013

Functional characterization and gene expression profiling of Drosophila melanogaster short dADA2b isoform-containing dSAGA complexes.

Tibor Pankotai, Nóra Zsindely, Edith E Vamos, Orbán Komonyi, László Bodai, Imre M Boros

Open access · goldAbstract read
In one paragraph

Article in BMC genomics, 2013. 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 31% 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. Article
  2. Article
  3. Review
  4. TheJournal of cell science · 2019
    Article
  5. Article
  6. 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

6 authors at 2 institutions in 1 country.

Tibor PankotaiDepartment of Biochemistry and Molecular Biology, University of Szeged, Középfasor 52, H-6726, Szeged, Hungary.
Nóra Zsindely
Edith E Vamos
Orbán Komonyi
László Bodai
Imre M Boros
University of Szeged · HUHUN-REN Szegedi Biológiai Kutatóközpont · HU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundADA2 proteins, together with ADA3, SGF29 and GCN5 form the acetyltransferase module of GNAT-type histone acetyltransferase complexes. ADA2b is present in the SAGA complex, which plays roles in various chromatin-related processes via histone H3 modifications and by other mechanisms.

resultsIn this report we present findings showing that during Drosophila melanogaster development two dADA2b isoforms (dADA2bS and dADA2bL) - which differ in their C-terminal domains - are expressed at various levels. Genetic complementation experiments indicate that dADA2bS alone can support development but cannot fully complement dAda2b mutations. In the presence of dADA2bS, the SAGA-specific histone H3 acetylation level is partially restored in dAda2b mutants. Comparison of whole transcriptome profiles of dAda2b null and dAda2bS transgene-carrier dAda2b null larvae indicates partial overlap between affected genes. mRNA levels corresponding to selected genes which are either up- or down-regulated in dAda2b mutants are altered by dADA2bS expression to different extents, ranging from complete restoration to wild type levels to no restoration at all. The short (dADA2bS) isoform of dADA2b seems to be more capable of restoring lost dSAGA functions that cause mRNA level up-regulation than those that lead to decreased mRNA levels.

conclusionsThe data presented here are in accord with results of genetic complementation experiments, and support the hypothesis that different isoforms of dADA2b contribute to the functional variations of dSAGA multiprotein HAT complexes.

Indexed as

Gene Expression ProfilingAcetylationAnimalsDrosophila melanogasterDrosophila ProteinsGene Expression Regulation, DevelopmentalHistone AcetyltransferasesHistonesIsoenzymesLarvaTranscription, GeneticAda2a protein, DrosophilaDrosophila ProteinsHistone AcetyltransferasesHistonesIsoenzymes

Identifiers

PMID23336284
PMCPMC3598691
OpenAlexW2077112265

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.