PXD050362-2

PXD050362 is an original dataset announced via ProteomeXchange.

Title	Improved Mass Spectrometry-based methods to study histone propionylation
Description	Histone post-translational modifications (PTMs) have crucial roles in a multitude of cellular processes, their aberrant levels have been linked with numerous diseases, including cancer. Although histone PTM investigations have focused so far on methylations and acetylations, alternative long-chain acylations emerged as new dimension, as they are linked to cellular metabolic states and affect gene expression through mechanisms distinct from those regulated by acetylation. Mass spectrometry (MS) is the most powerful, comprehensive and unbiased method to study histone PTMs. Typical protocols for histone PTM analysis do not allow identification of naturally occurring propionylation and butyrylation. Here, we present improved state-of-the-art sample preparation and analysis protocols to quantitate these classes of modifications. After testing different derivatization methods coupled to protease digestion, we profiled common histone PTMs and histone acylations in seven mouse tissues and human normal and tumor breast clinical samples, obtaining a map of propionylations and butyrylations found in different tissue contexts. A quantitative histone PTM analysis also revealed a contribution of histone acylations in discriminating different tissues and breast cancer samples from the normal counterpart.
HostingRepository	PRIDE
AnnounceDate	2024-10-22
AnnouncementXML	Submission_2024-10-22_06:49:26.204.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Roberta Noberini
SpeciesList	scientific name: Mus musculus (Mouse); NCBI TaxID: 10090; scientific name: Homo sapiens (Human); NCBI TaxID: 9606;
ModificationList	monomethylated residue; acylated residue; acetylated residue; N6,N6,N6-trimethyl-L-lysine; N6,N6-dimethyl-L-lysine
Instrument	Q Exactive HF; Q Exactive Plus

Revision	Datetime	Status	ChangeLog Entry
0	2024-03-05 06:36:44	ID requested
1	2024-10-07 13:52:21	announced
⏵ 2	2024-10-22 06:49:27	announced	2024-10-22: Updated project metadata.

10.1016/j.mcpro.2024.100799;

submitter keyword: histone post-translational modifications, propionylation, acylation

Tiziana Bonaldi
contact affiliation	European Instutute of Oncology, Milan
contact email	tiziana.bonaldi@ieo.it
lab head
Roberta Noberini
contact affiliation	Istituto Europeo di Oncologia
contact email	roberta.noberini@ieo.it
dataset submitter

Dataset FTP location NOTE: Most web browsers have now discontinued native support for FTP access within the browser window. But you can usually install another FTP app (we recommend FileZilla) and configure your browser to launch the external application when you click on this FTP link. Or otherwise, launch an app that supports FTP (like FileZilla) and use this address: ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2024/07/PXD050362

PRIDE project URI

• PRIDE
  1. PXD050362
     1. Label: PRIDE project
     2. Name: Improved Mass Spectrometry-based methods to study histone propionylation