PXD014452-1

PXD014452 is an original dataset announced via ProteomeXchange.

Title	Histone acetyltransferase 2 links H4 acetylation, H2A.Z deposition and transcription start site-choice in African trypanosomes
Description	Both, acetylation of histones and of histone variant H2A.Z are conserved features of eukaryotic transcription start sites (TSSs) and both features appear to be critical for correct transcription initiation. However, complex patterns of transcriptional regulation have complicated the establishment of functional links between histone acetylation, H2A.Z deposition and their importance in transcription regulation. To elucidate these links, we took advantage of the unusual genome organization in Trypanosoma brucei, a highly divergent eukaryote. In T. brucei genes are organized in long polycistronic transcription units, drastically reducing the sites of transcription initiation. Employing a highly sensitive and quantitative mass-spectrometry-based approach, we quantified the genome-wide histone acetylation and methylation pattern and identified various acetyl and methyl marks exclusively enriched at TSSs In addition, we show that deletion of histone acetyltransferase 2 results in a loss of H4 acetylation at TSSs, a loss of H2A.Z deposition at TSSs and a shift in the sites of transcription initiation. Combined, our findings demonstrate an evolutionary conserved link between histone H4 acetylation, H2A.Z deposition and RNA transcription initiation.
HostingRepository	PRIDE
AnnounceDate	2020-03-24
AnnouncementXML	Submission_2020-03-24_08:38:07.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Benedikt Brink
SpeciesList	scientific name: Trypanosoma brucei; NCBI TaxID: 5691;
ModificationList	methylated residue; acetylated residue
Instrument	Orbitrap Fusion

Revision	Datetime	Status	ChangeLog Entry
0	2019-07-01 07:17:45	ID requested
⏵ 1	2020-03-24 08:38:09	announced

Kraus AJ, Vanselow JT, Lamer S, Brink BG, Schlosser A, Siegel TN, Distinct roles for H4 and H2A.Z acetylation in RNA transcription in African trypanosomes. Nat Commun, 11(1):1498(2020) [pubmed]

ElBashir R, Vanselow JT, Kraus A, Janzen CJ, Siegel TN, Schlosser A, Fragment ion patchwork quantification for measuring site-specific acetylation degrees. Anal Chem, 87(19):9939-45(2015) [pubmed]

submitter keyword: histone acetylation H2A.Z transcription trypanosome

Prof. T. Nicolai Siegel
contact affiliation	Department of Veterinary Sciences, Experimental Parasitology Ludwig-Maximilians-Universität München Leopoldstr. 5 80802 Munich Germany Biomedical Center Munich, Physiological Chemistry Ludwig-Maximilians-Universität München Großhaderner Str. 9 82152 Planegg-Martinsried Germany
contact email	n.siegel@lmu.de
lab head
Benedikt Brink
contact affiliation	LMU Munich
contact email	b.brink@lmu.de
dataset submitter

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PRIDE project URI

• PRIDE
  1. PXD014452
     1. Label: PRIDE project
     2. Name: Histone acetyltransferase 2 links H4 acetylation, H2A.Z deposition and transcription start site-choice in African trypanosomes