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S. venezuelae HupS protein acetylated lysine mapping via bottom-up LC-MS

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 identify post-translationally acetylated lysine residues of HupS via bottom-up LC-MS. Two approaches were uptaken. One was based on HupS enrichment from a strain expressing a recombinant HupS with a C-terminal FLAG tag (TM015) via an antiFLAG pull-down, and the other relied on a proteome-wide search of acetylated peptides in a WT strain lysate. Controls for spectral false-positives were also carried out in parallel, which were an antiFLAG pull-down with a WT strain, and a proteome-wide search of acetylated peptides in a HupS deletion mutant strain (ΔhupS) lysate. 5 lysine acetylation sites were confidently determined for the HupS protein within this study, them being Lys51, Lys85, Lys104, Lys119, and either Lys193 or Lys194.

INSTRUMENT(S): Synapt MS

ORGANISM(S): Streptomyces Venezuelae Atcc 10712

TISSUE(S): Endospore

SUBMITTER: Michał Tracz

LAB HEAD: Michal Tracz

PROVIDER: PXD050776 | Pride | 2024-06-03

REPOSITORIES: Pride

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			Action	DRS
	240216_ZMM_MSZ_1_r1_nr10.raw.zip	Raw
	240216_ZMM_MSZ_1_r2_nr10.raw.zip	Raw
	240216_ZMM_MSZ_2_r1_nr10.raw.zip	Raw
	240216_ZMM_MSZ_2_r2_nr10.raw.zip	Raw
	240307_ZMM_MSZ_TM015_3.raw.zip	Raw

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