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N-terminal and whole-protein profiling on R-catcher-enriched samples

ABSTRACT: The project involves the purification of Nt-arginylated proteins and their interacting partners in Human cell line HMEC and T-47D. The purification was done with R-catcher.

INSTRUMENT(S):

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Permanent Cell Line Cell, Cell Culture

DISEASE(S): Breast Cancer

SUBMITTER: Shinyeong Ju

LAB HEAD: Cheolju Lee

PROVIDER: PXD064220 | Pride | 2025-09-29

REPOSITORIES: Pride

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Dataset's files

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			Action	DRS
	230516_RCATCHER_GLOBAL_E1F01.mzML	Mzml
	230516_RCATCHER_GLOBAL_E1F01.pepXML	Pepxml
	230516_RCATCHER_GLOBAL_E1F02.mzML	Mzml
	230516_RCATCHER_GLOBAL_E1F02.pepXML	Pepxml
	230516_RCATCHER_GLOBAL_E1F03.mzML	Mzml

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1 - 5 of 194

Publications

ATE1 promotes breast cancer progression via arginylation-dependent regulation of MAPK-MYC signaling.

Nawale Laxman L Ju Shinyeong S Kim Jung Gi JG Soung Nak Kyun NK Kim Bo Yeon BY Lee Cheolju C Cha-Molstad Hyunjoo H

Cell communication and signaling : CCS 20250902 1

<h4>Background</h4>Arginyl-tRNA-protein transferase (ATE1) catalyzes N-terminal arginylation, a regulatory protein modification implicated in various cellular processes, including proliferation, apoptosis, and migration. Although ATE1 has context-dependent roles in cancer, its specific function in breast cancer remains unclear. This study investigates the oncogenic role of ATE1 across multiple breast cancer subtypes and its underlying molecular mechanisms.<h4>Methods</h4>ATE1 expression in breas ...[more]

PMID: 40898325

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plasma membrane anchored NAA60 N-terminal acetylation profiling in Arabidopsis thaliana

Project description:N-terminal acetylation (NTA) is one of the most abundant protein modifications in eukaryotes and is catalysed in humans by seven N-acetyltransferases. AtNAA60 localizes to the plasma membrane in vivo by an α-helical membrane anchor at its C-terminus. In this study, we investigated the Arabidopsis thaliana N-terminal acetylome in leaf cells of naa60-1 to identify AtNAA60 substrates in vivo using the SILProNAQ approach.

2020-07-15 | PXD016494 | Pride

AtNAA50 N-terminal acetylation profiling using A. thaliana naa50 KO mutants

Project description:N-terminal acetylation is one of the most abundant protein modifications in eukaryotes and is catalysed in humans by seven N-terminal acetyltransferases. AtNAA50 interreact with the NatA complex (NAA10 and NAA15) to form the NatE complex. In this study, we investigated the Arabidopsis thaliana N-terminal acetylome in leaf cells with KO naa50 gene to identify in vivo specific substrates using the SILProNAQ approach.

2020-07-15 | PXD017770 | Pride

Transcription profiling of E. coli BW25113 fhlAL/pCA24N-FhlA133 vs fhlA/pCA24N-FhlA in modified-complex 20 mM formate at 37A?C

Project description:Variant FhlA133 (Q11H, L14V, Y177F, K245R, M288K, and I342F) had eight- fold higher hydrogen production than FhlA wild-type under 30 min of anaerobic incubation in modified-complex 20 mM formate at 37ÂºC. The mechanism by which the FhlA133 mutations increase hydrogen production is by increasing the transcription of all of the genes activated by the native FhlA (FHL complex). Experiment Overall Design: Strains: E. coli BW25113 fhlA/pCA24N-FhlA wild-type and E. coli BW25113 fhlA/pCA24N-FhlA133 (Q11H, L14V, Y177F, K245R, M288K, and I342F). Experiment Overall Design: Medium: Modified-complex 20 mM formate Experiment Overall Design: 1 mL of overnight culture in modified - complex 20 mM formate + Cm 30 Âµg/mL was inoculated in 9 mL of fresh modified - complex 20 mM formate + Cm 30 Âµg/mL and incubated anaerobically at 37oC in 27 mL glass vials. Experiment Overall Design: Time: 30 minutes Experiment Overall Design: Cell type: Suspension

2009-12-19 | E-GEOD-13902 | biostudies-arrayexpress

N-terminal acetylation by NatB in Arabidopsis thaliana

Project description:N-terminal acetylation (NTA) is one of the most abundant protein modifications in eukaryotes and is catalysed in humans by seven N-acetyltransferases. In this study, we investigated the Arabidopsis thaliana NatB catalytic (NAA20) and auxiliary subunit (NAA25) and their influence on protein N-terminal acetylation using the SILProNAQ approach

2019-11-21 | PXD016209 | Pride

Global acetylation profiling for the Arabidopsis thaliana the N-acetyltransferase NAA50 in the NatA complex.

Project description:N-terminal acetylation is one of the most abundant protein modifications in eukaryotes and is catalysed in humans by seven N-terminal acetyltransferases. AtNAA50 interreact with the NatA complex (NAA10 and NAA15) to form the NatE complex. In this study, we investigated the activity of this catalytic subunit using the global acetylome profiling test (GAP test).

2020-07-15 | PXD017767 | Pride

Global acetylation profiling for the Arabidopsis thaliana plasma membrane anchored NAA60 N-terminal acetyltransferase

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2020-07-15 | PXD016533 | Pride

Global acetylation profiling for multiple Arabidopsis thaliana plastid N-terminal acetyltransferases

Project description:Protein acetylation is a universally conserved modification occurring on N-termini (N-Terminal acetylation, NTA). Although recent reports indicate that NTA occur frequently in plant plastids, little is known about the machinery involved in plastid acetylation and why these modifications are that frequent in this organelle. Searches for new putative N-acetyltransferase genes in Arabidopsis thaliana highlighted eight putative candidates located at plastid subcellular location. In this study, we investigated the N-acetyltransferase specificity of these enzymes using the global acetylome profiling test (GAP test).

2020-07-13 | PXD016205 | Pride

Identification and characterization of the first Nα-acetyltransferase in plastids

Project description:Protein Nα-terminal acetylation represents one of the most abundant protein modifications of higher eukaryotes. In humans, six Nα-acetyltransferases (Nats) are responsible for the acetylation of approximately 80% of the cytosolic proteins. N-terminal protein acetylation has not been evidenced in organelles of metazoans, but in higher plants, it is a widespread modification not only in the cytosol but also in the chloroplast. In this study, we identify and characterize the first organellar-localized Nat in eukaryotes. A primary sequence-based search in Arabidopsis thaliana revealed seven putatively plastid-localized Nats of which AT2G39000 (AtNAA70) showed the highest conservation of the acetyl-CoA binding pocket. The chloroplastic localization of AtNAA70 was demonstrated by transient expression of AtNAA70:YFP in Arabidopsis mesophyll protoplasts. Homology modeling uncovered a significant conservation of tertiary structural elements between human HsNAA50 and AtNAA70. The in vivo acetylation activity of AtNAA70 was demonstrated on a number of distinct protein N alpha-termini with a newly established Nat-activity global profiling after expression of AtNAA70 in E. coli. AtNAA70 predominately acetylated proteins starting with M, A, S, and T, providing an explanation for most protein N-termini acetylation events found in chloroplasts.

2015-06-29 | PXD001947 | Pride

Pathology tissue-quantitative mass spectrometry analysis to profile histone post-translational modification patterns in patient samples

Project description:Histone post-translational modifications (hPTMs) generate a complex combinatorial code that has been implicated with various pathologies, including cancer. Dissecting such a code in physiological and diseased states may be exploited for epigenetic biomarker discovery, but hPTM analysis in clinical samples has been hindered by technical limitations. Here, we developed a method (PAThology tissue Histones by Mass Spectrometry - PAT-H-MS) that allows to perform a comprehensive, unbiased and quantitative MS-analysis of hPTM patterns on formalin-fixed paraffin-embedded (FFPE) samples. In pairwise comparisons, histone extracted from FFPE tissues showed patterns similar to fresh frozen samples for 24 differentially modified peptides from histone H3. In addition, when coupled with a histone-focused version of the super-SILAC approach, this method allows the accurate quantification of modification changes among breast cancer patient samples. We applied this strategy to the analysis of breast cancer subtypes, revealing significant changes between Luminal A and Triple Negative samples in peptides containing K27me3 and K9me3, which were validated by immunohistochemistry and western blot analysis. These results pave the way for retrospective epigenetic studies that combine the power of MS-based hPTM analysis with the extensive clinical information associated with FFPE archives.

2015-10-14 | PXD002669 | Pride

Transcription profiling by array of E. coli NCTC 9001 challenged with four different cationic antimicrobial peptides

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