Evidence map›Paper›PMID 26586808›Full record

ArticleNucleic acids research2016

A novel role for the histone acetyltransferase Hat1 in the CENP-A/CID assembly pathway in Drosophila melanogaster.

Mark Boltengagen, Anming Huang, Anastasiya Boltengagen, Lukas Trixl, Herbert Lindner, Leopold Kremser, Martin Offterdinger, Alexandra Lusser

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
1.7field-weighted citation impact, top 16% 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

26 citing papers in PubMed, 37 citations in OpenAlex.

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  7. Epigenetic Regulation of ALS and CMT: A Lesson fromInternational journal of molecular sciences · 2021
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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 2 institutions in 1 country.

Mark BoltengagenDivision of Molecular Biology, Biocenter, Medical University of Innsbruck, 6020 Innsbruck, Austria.
Anming HuangDivision of Molecular Biology, Biocenter, Medical University of Innsbruck, 6020 Innsbruck, Austria.
Anastasiya BoltengagenDivision of Molecular Biology, Biocenter, Medical University of Innsbruck, 6020 Innsbruck, Austria.
Lukas TrixlDivision of Molecular Biology, Biocenter, Medical University of Innsbruck, 6020 Innsbruck, Austria.
Herbert LindnerDivision of Clinical Biochemistry, Biocenter, Medical University of Innsbruck, 6020 Innsbruck, Austria.
Leopold KremserDivision of Clinical Biochemistry, Biocenter, Medical University of Innsbruck, 6020 Innsbruck, Austria.
Martin OffterdingerDivision of Neurobiochemistry, Biocenter, Medical University of Innsbruck, 6020 Innsbruck, Austria.
Alexandra LusserDivision of Molecular Biology, Biocenter, Medical University of Innsbruck, 6020 Innsbruck, Austria alexandra.lusser@i-med.ac.at.
Innsbruck Medical University · ATUniversität Innsbruck · AT

Funding

Austrian Science Fund FWF Y 275
6 · The paper itself

Abstract

The incorporation of CENP-A into centromeric chromatin is an essential prerequisite for kinetochore formation. Yet, the molecular mechanisms governing this process are surprisingly divergent in different organisms. While CENP-A loading mechanisms have been studied in some detail in mammals, there are still large gaps to our understanding of CENP-A/Cid loading pathways in Drosophila. Here, we report on the characterization and delineation of at least three different CENP-A preloading complexes in Drosophila. Two complexes contain the CENP-A chaperones CAL1, FACT and/or Caf1/Rbap48. Notably, we identified a novel complex consisting of the histone acetyltransferase Hat1, Caf1 and CENP-A/H4. We show that Hat1 is required for proper CENP-A loading into chromatin, since knock-down in S2 cells leads to reduced incorporation of newly synthesized CENP-A. In addition, we demonstrate that CENP-A/Cid interacts with the HAT1 complex via an N-terminal region, which is acetylated in cytoplasmic but not in nuclear CENP-A. Since Hat1 is not responsible for acetylation of CENP-A/Cid, these results suggest a histone acetyltransferase activity-independent escort function for Hat1. Thus, our results point toward intriguing analogies between the complex processing pathways of newly synthesized CENP-A and canonical histones.

Indexed as

AcetylationAmino Acid SequenceAnimalsCarrier ProteinsCell LineCell NucleusCentromere Protein AChromatinCytoplasmDNA-Binding ProteinsDrosophila melanogasterDrosophila ProteinsGene Expression RegulationHistone AcetyltransferasesHistonesKinetochoresCaf1-55 protein, DrosophilaCal1 protein, DrosophilaCarrier ProteinsCentromere Protein AChromatinCid protein, DrosophilaDNA-Binding ProteinsDrosophila ProteinsFACT protein, DrosophilaHistone Acetyltransferaseshistone acetyltransferase type B complexHistonesRetinoblastoma-Binding Protein 4

Identifiers

PMID26586808
PMCPMC4797270
OpenAlexW2218848041

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.