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One-step N-terminomics based on isolation of protein N-terminal peptides from LysargiNase digests by tip-based strong cation exchange chromatography
Open accessPreprint — published as 10.1016/j.mcpro.2024.100820
Abstract
We have developed a one-step isolation method for protein N-terminal peptides from LysargiNase digests by pipette tip-based strong cation exchange (SCX) chromatography. This CHAMP-N (CHromatographic AMplification of Protein N-terminal peptides) method using disposable and parallel-processable SCX tips instead of conventional HPLC SCX columns facilitates simple, sensitive and high-throughput N-terminomic profiling without sacrificing the high identification numbers and selectivity achieved by the HPLC-based method. By applying the CHAMP-N method to HEK293T cells, we identified novel cleavage sites for signal and transit peptides, and non-canonical translation initiation sites. Finally, for proteome-wide terminomics, we present a simple and comprehensive N-and C-terminomics platform employing three different tip-based approaches, including CHAMP-N, in which protease digestion and one-step isolation by tip LC are commonly used to achieve complementary terminome coverages.
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How many human proteoforms are there?
Aebersold, R., Agar, J. N., Amster, I. J., Baker, M. S., Bertozzi, C. R., Boja, E. S., Costello, C. E., Cravatt, B. F., Fenselau, C., Garcia, B. A., et al. (2018) · Nature Chemical Biology · doi:10.1038/nchembio.2576 · Cited by 907
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Research works printed but not linked: 36
- 2019, A five-level classification system for proteoform identifications, Nat. Methods, 16, 939, 10.1038/s41592-019-0573-x · DOI
- Consortium for Top-Down Proteomics, 2021, The Human Proteoform Project: Defining the human proteome, Sci Adv, 7, eabk0734, 10.1126/sciadv.abk0734 · DOI · Paper page
- 10.1186/1752-153X-3-11 · DOI
- 2019, Novel oncogene 5MP1 reprograms c-Myc translation initiation to drive malignant phenotypes in colorectal cancer, EBioMedicine, 44, 387, 10.1016/j.ebiom.2019.05.058 · DOI
- 10.1101/gad.8.20.2441 · DOI
- 10.1016/0092-8674(88)90507-7 · DOI · Paper page
- 10.1007/s12017-009-8104-z · DOI · Paper page
- 10.1073/pnas.1816596116 · DOI · Paper page
- 10.1038/nbt810 · DOI
- 10.1038/nbt.1611 · DOI
- Hanna, R. , Rozenberg, A. , Saied, L. , Ben-Yosef, D. , Lavy, T. , and Kleifeld, O . (2023) In-Depth Characterization of Apoptosis N-Terminome Reveals a Link Between Caspase-3 Cleavage and Posttranslational N-Terminal Acetylation. Mol. Cell. Proteomics 22, · DOI
- 2021, Isolation of Acetylated and Unmodified Protein N-Terminal Peptides by Strong Cation Exchange Chromatographic Separation of TrypN-Digested Peptides, Mol. Cell. Proteomics, 20, 100003, 10.1074/mcp.TIR120.002148 · DOI
- 2022, One-Step Isolation of Protein C-Terminal Peptides from V8 Protease-Digested Proteins by Metal Oxide-Based Ligand-Exchange Chromatography, Anal. Chem, 94, 944, 10.1021/acs.analchem.1c03722 · DOI
- 2021, Exploring the landscape of ectodomain shedding by quantitative protein terminomics, iScience, 24, 102259, 10.1016/j.isci.2021.102259 · DOI · Paper page
- 10.1021/ac9004309 · DOI
- 2010, Peptide orientation affects selectivity in ion-exchange chromatography, Anal. Chem, 82, 5253, 10.1021/ac100651k · DOI
- 10.1074/mcp.M900463-MCP200 · DOI
- 2021, A protocol for analyzing the protein terminome of human cancer cell line culture supernatants, STAR Protoc, 2, 100682, 10.1016/j.xpro.2021.100682 · DOI
- 10.1021/pr700658q · DOI
- 10.1021/ac026117i · DOI
- 10.1038/nprot.2007.261 · DOI · Paper page
- 10.1016/S0021-9673(02)01402-4 · DOI
- 10.1021/acs.analchem.8b02233 · DOI
- 2008, MaxQuant enables high peptide identification rates, individualized p, p.b.-range mass accuracies and proteome-wide protein quantification. Nat. Biotechnol, 26, 1367
- 10.1021/pr101065j · DOI
- 2014, Characterization and usage of the EASY-spray technology as part of an online 2D SCX-RP ultra-high pressure system, Analyst, 139, 6520, 10.1039/C4AN01568A · DOI
- 2016, Development of Online pH Gradient-Eluted Strong Cation Exchange Nanoelectrospray-Tandem Mass Spectrometry for Proteomic Analysis Facilitating Basic and Histidine-Containing Peptides Identification, Anal. Chem, 88, 583, 10.1021/acs.analchem.5b04000 · DOI
- 10.1021/acs.analchem.6b01232 · DOI
- 10.1016/j.molcel.2019.02.007 · DOI
- 10.1016/j.cell.2011.10.002 · DOI · Paper page
- 10.1073/pnas.1207846109 · DOI
- 10.1126/science.aay0262 · DOI
- 2021, Combinatorial analysis of translation dynamics reveals eIF2 dependence of translation initiation at near-cognate codons, Nucleic Acids Res, 49, 7298, 10.1093/nar/gkab549 · DOI
- Almagro Armenteros, J. J. , Salvatore, M. , Emanuelsson, O. , Winther, O. , von Heijne, G. , Elofsson, A. , and Nielsen, H. (2019) Detecting sequence signals in targeting peptides using deep learning. Life Sci Alliance 2, · DOI
- 2022, SignalP 6.0 predicts all five types of signal peptides using protein language models, Nat. Biotechnol, 40, 1023, 10.1038/s41587-021-01156-3 · DOI
- 10.1093/nar/gku1012 · DOI
Metadata
- Authors
- Morikawa, K., Nishida, H., Imami, K., & Ishihama, Y.
- Affiliations
- Kyoto University (JP)
- Corresponding author
- Ishihama, Yasushi
- Venue
- Molecular & Cellular Proteomics
- Publisher
- openRxiv
- Published
- 2024-02-07
- Volume
- 23
- Issue
- 9
- Pages
- 100820-100820
- ISSN
- 1535-9476 (ISSN-L)
- PMC
- PMC11382313
- OpenAlex
- W4401056525
- Cited by
- 10
- References
- 1
- Citations by year
- 2026: 5 · 2025: 5
- FWCI
- 1.25
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- cc-by
- Locations
- Molecular & Cellular Proteomics (publishedVersion, cc-by)
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Funders
- Japan Agency for Medical Research and Development (CREST, No. JP18gm1010010, JP18gm1010010)
- Japan Society for the Promotion of Science (21H02459, 23H04924, 23K18185, 20H03241, CREST)
- Core Research for Evolutional Science and Technology (JPMJCR1862, JP18gm1010010)
- Topics
- Physical Sciences › Chemistry › Spectroscopy › Advanced Proteomics Techniques and Applications
- Physical Sciences › Chemistry › Spectroscopy › Mass Spectrometry Techniques and Applications
- Physical Sciences › Chemistry › Organic Chemistry › Chemical Synthesis and Analysis
- Keywords
- N-terminomics, strong cation exchange chromatography, signal peptide cleavage site, proteolytic digestion
- MeSH terms
- Chromatography, Ion Exchange, Humans, Peptides, Proteome, Proteomics, HEK293 Cells
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