Dataset Information

In-depth Profiling and Quantification of the Acetylproteome in Hepatocellular Carcinoma with a Trapped Ion Mobility Mass Spectrometer

ABSTRACT: In this study, we employed an integrated proteomics and acetyl-proteomics strategy to characterize of 8 tumors and 8 matched normal adjacent tissues (NATs) with 4D proteomics technology. Proteomics analysis identified a total of 6551 proteins, of which 5411 proteins were quantified across all samples. A total of 8789 acetylation sites on 2348 proteins were identified, of which 5112 sites of 1620 proteins contained quantitative information.

INSTRUMENT(S): timsTOF Pro

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Liver

SUBMITTER: jia xu

LAB HEAD: Ruibing Chen

PROVIDER: PXD026729 | Pride | 2022-07-02

REPOSITORIES: pride

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In-depth Profiling and Quantification of the Lysine Acetylome in Hepatocellular Carcinoma with a Trapped Ion Mobility Mass Spectrometer.

Xu Jia J Guan Xinyu X Jia Xiaodong X Li Hongyan H Chen Ruibing R Lu Yinying Y

Molecular & cellular proteomics : MCP 20220608 8

Hepatocellular carcinoma (HCC) is the third most common cause of cancer-related death worldwide with limited therapeutic options. Comprehensive investigation of protein posttranslational modifications in HCC is still limited. Lysine acetylation is one of the most common types of posttranslational modification involved in many cellular processes and plays crucial roles in the regulation of cancer. In this study, we analyzed the proteome and K-acetylome in eight pairs of HCC tumors and normal adja ...[more]

PMID: 35688384

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Project description:Co-translational N-terminal (Nt-) acetylation of nascent polypeptides is catalyzed by N-terminal acetyltransferases (NATs). The very N-terminal amino acid sequence is the major factor determining whether or not a given protein is Nt-acetylated. In humans, six different NATs, denoted NatA-NatF, are identified. In the current study we used N-terminal COFRADIC analysis to define the in vivo substrate specificity of Naa50 (Nat5)/NatE as this has long remained elusive. Three yeast strains were generated; a control strain endogenously expressing yNaa50, a deletion strain depleted of yNaa50 and a strain deleted of yNaa50 but ectopically expressing human Naa50. When comparing the Nt-acetylation status of different N-termini in the control strain with the deletion strain, a reduction in Nt-acetylation for several yeast proteins was observed. To our surprise, these substrates were not of the predicted NatE-type substrates, but rather canonical NatA substrates. Further, ectopic expression of hNaa50 mainly resulted in the Nt-acetylation of a selected class of otherwise Nt-free yeast N-termini besides increasing the degree of Nt-acetylation of several other yeast proteins, and as such (partially) complementing those N-termini displaying reduced Nt-acetylation upon yNAA50-deletion. The preferred substrates of hNaa50 were predominantly Met-starting N-termini including Met-Lys-, Met-Val-, Met-Ala-, Met-Tyr-, Met-Phe-, Met-Leu-, Met-Ser- and Met-Thr, and highly overlapped with the previously identified human Naa60/NatF substrate specificity profile. Identification of several hNaa50 substrates with a small amino acid in the second position also revealed a potential interplay between the NATs and methionine aminopeptidases (MetAPs). The initiator Methionine (iMet) is normally cleaved off by MetAPs when the second amino acid is small, but our in vitro data suggest that in contrast to a free iMet, an Nt-acetylated iMet is not hydrolyzed by MetAPs. Thus, Naa50-mediated Nt-acetylation may potentially act as a mechanism to retain the iMet of proteins with a small amino acid at the second position that normally would be hydrolyzed.

			Action	DRS
	Ac_N1.d.rar	Other
	Ac_N2.d.rar	Other
	Ac_N3.d.rar	Other
	Ac_N4.d.rar	Other
	Ac_N5.d.rar	Other