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Identification of recombinant HupS protein in vitro acetylation extent

ABSTRACT: 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).

INSTRUMENT(S): Synapt MS

ORGANISM(S): Streptomyces Venezuelae

SUBMITTER: Michał Tracz

LAB HEAD: Michal Tracz

PROVIDER: PXD048203 | Pride | 2024-06-03

REPOSITORIES: Pride

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Dataset's files

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			Action	DRS
	230519_ZMM_JDU_HUPS_minus_10x.raw.zip	Raw
	231002_ZMM_JDU_HupsAc_r1.raw.zip	Raw
	ME1_25500_27500.tiff	Other
	ME1_full.tiff	Other
	Raw_spectra_600_1600.tiff	Other

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