PXD048203

PXD048203 is an original dataset announced via ProteomeXchange.

Title	Identification of recombinant HupS protein in vitro acetylation extent
Description	Nucleoid-associated proteins (NAPs) are critical during the process of chromatin compaction in Streptomyces soil bacteria. HupS is one of the two NAPs encoded in the Streptomyces genome. Its unique C-terminal domain, rich in lysine repeats (LR domain), is alike to the H2B histone found in eukaryotic cells or the HupB protein found in Mycobacterium. Project study aim was to investigate if the lysine residues of the HupS LR domain undergo the posttranslational reversible lysine acetylation process. Mass spectrometry approach was employed in order to identify the number of acetyl groups attached to the recombinantly produced and subsequently purified HupS protein after it was subdue to an in vitro acetylation reaction with acetyl phosphate (AcP).
HostingRepository	PRIDE
AnnounceDate	2024-06-03
AnnouncementXML	Submission_2024-06-03_02:59:23.471.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Michał Tracz
SpeciesList	scientific name: Streptomyces venezuelae; NCBI TaxID: 54571;
ModificationList	acetylated residue
Instrument	Synapt MS

Revision	Datetime	Status	ChangeLog Entry
0	2024-01-02 09:48:12	ID requested
⏵ 1	2024-06-03 02:59:23	announced

10.1093/NAR/GKAE418;

submitter keyword: LC-MS, acetylation, NAP protein, HupS, protein modification, Streptomyces, intact protein mass analysis

Michal Tracz
contact affiliation	Laboratory of Protein Mass Spectrometry, Faculty of Biotechnology, University of Wroclaw, Poland
contact email	michal.tracz2@uwr.edu.pl
lab head
Michał Tracz
contact affiliation	Laboratory of Protein Mass Spectrometry, Faculty of Biotechnology, University of Wroclaw
contact email	michal.tracz2@uwr.edu.pl
dataset submitter

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PRIDE project URI

• PRIDE
  1. PXD048203
     1. Label: PRIDE project
     2. Name: Identification of recombinant HupS protein in vitro acetylation extent