New ProteomeXchange dataset PXD057969

[ProteomeCentral Agent]

Dear ProteomeXchange subscriber, a new ProteomeXchange dataset is being announced. To see more information, click here:

https://proteomecentral.proteomexchange.org/dataset/PXD057969

Summary of dataset

Status: new
Identifier: PXD057969
HostingRepository: PRIDE
Species: Homo sapiens
Title: KDM3A catalysed formation of hydroxyacetyl-lysine on histone H3K9
Submitter: Simone Sidoli
LabHead: Simone Sidoli
Description: Histone modifications, including N-lysine acetylation and methylation, play critical roles in eukaryotic transcription. The addition of acetyl- and methyl-groups and removal of acetyl-groups involves redox neutral reactions, whereas demethylation is O2 dependent, a reaction with potential to enable O2 availability mediated regulation, as occurs for reactions catalysed by the 2-oxoglutarate dependent hypoxia-inducible factor (HIF) hydroxylases. A screen for substrates of the HIF-regulated Jumonji-C (JmjC) lysine demethylase KDM3A led to the finding that purified recombinant KDM3A catalyses oxidation of the N-acetyl group of Lys-9 of histone H3 giving an N-hydroxyacetyl-lysine residue. Studies employing a N-hydroxyacetyl-lysine selective antibody and mass spectrometry support the cellular relevance of N-hydroxyacetyl-lysine. The combined biochemical and cellular results reveal evidence for an unanticipated O2-mediated link between histone lysine N-acetyla
tion and JmjC catalysis. Future work can explore the biological significance of N-hydroxyacetylation, including in the hypoxic response where KDM3A plays a role in regulating HIF target genes.

HTML_URL: https://proteomecentral.proteomexchange.org/dataset/PXD057969
XML_URL: https://proteomecentral.proteomexchange.org/dataset/PXD057969&outputMode=XML