Dataset Information

LC-MS targeting the rpL40-Lys22 spanning peptide in rpL40-immunoprecipitated KKLS human gastric cancer cell extracts

ABSTRACT: We identified SMYD5 (SET and MYND Domain-Containing Protein 5) physiologically methylates core ribosomal protein L40 at lysine 22 (rpL40K22me3). rpL40K22me3 depletion upon SMYD5 knockdown in GAC KKLS cells was observed by targeted-mass spectrometry of immunoprecipitated rpL40.

INSTRUMENT(S):

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Gastric Adenocarcinoma Cell

SUBMITTER: Juhyung Park

LAB HEAD: Or Gozani

PROVIDER: PXD052358 | Pride | 2024-06-04

REPOSITORIES: Pride

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Dataset's files

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			Action	DRS
	20231105_EBZ_Gozani_KKLS_sgControl_rpL40_IP_Chymo.raw	Raw
	20231105_EBZ_Gozani_KKLS_sgSMYD5_rpL40_IP_Chymo.raw	Raw
	KKLS_rpL40_targeted-ms_results.pdf	Pdf
	checksum.txt	Txt

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Project description:Chromatin structure and function is maintained by dynamic protein-protein and protein-nucleic acid interactions. Histones are a family of proteins that are abundant chromatin constituents and that carry numerous post-translational modifications (PTMs). Histone PTMs mediate a variety of biological activities, including recruitment of enzymatic readers, writers and erasers that modulate protein activities, DNA replication, transcription and repair. Individual histone molecules contain multiple co-existing PTMs some of which exhibit crosstalk, i.e. coordinated or mutually exclusive activities. We here present an integrated experimental and computational approach for systems level molecular characterization of PTMs and PTM crosstalk. Using wildtype and engineered mouse embryonic stem cells with perturbations in the Polycomb Repressive Complex 1 (PRC1, suz12-/-), PRC2 (Ring1A/b-/-) and DNA methyltransferases (Dnmt1/3a/3b-/-) we performed comprehensive PTM analysis of histone H3 tails. We identified unique histone H3 PTM features of each of the four cell lines and we detected common combinatorial PTM features across cell lines. Using quantitative middle-down proteomics combined with probabilistic and statistical data analysis we extracted histone H3 PTM profiles for all four mESC systems. PTM crosstalk emerged as mutually exclusive histone PTMs or coordinately regulated PTMs independent of histone peptide abundance in the four model systems. We detected positive crosstalk between adjacent mono-methylated marks but strong negative crosstalk among most of the seven characterized di- and tri-methylations on lysines. We report novel features of PTM interplay involving hitherto poorly characterized arginine methylation and lysine methylation sites in histone H3, including H3R2me, H3R8me and H3K37me, which exhibited specific PTM codes suggesting a particular role in chromatin. All histone H3 PTM data is available in our publicly available CrossTalkDB repository at http://crosstalkdb.bmb.sdu.dk

Dataset Information

LC-MS targeting the rpL40-Lys22 spanning peptide in rpL40-immunoprecipitated KKLS human gastric cancer cell extracts

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