Detection of C-terminal peptide of proteins using isotope coding strategies

Julka, Samir; Dielman, Demetrius; Young, Scott A.

doi:10.1016/j.jchromb.2008.09.012

Cited by 12 publications

(15 citation statements)

References 25 publications

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“…Finally, the cleavage site was confirmed by mass spectrometry. Therefore, in vitro cleavage was performed in the presence of H 2 18 O and gel‐pieces of the full length and resulting proteolytic fragments were analysed by liquid chromatography coupled with tandem mass spectrometry (LC–MS/MS) and isotope peak distribution was calculated (Julka et al , 2008). Incorporation of 18 O at the C‐terminal carboxyl group of the N‐terminal CYLD fragment, and its corresponding tryptic peptide, confirms that MALT1 directly cleaves CYLD at arginine 324 (Figure 4).…”

Section: Resultsmentioning

confidence: 99%

T-cell receptor-induced JNK activation requires proteolytic inactivation of CYLD by MALT1

et al. 2011

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The paracaspase mucosa-associated lymphoid tissue 1 (MALT1) is central to lymphocyte activation and lymphomagenesis. MALT1 mediates antigen receptor signalling to NF-jB by acting as a scaffold protein. Furthermore, MALT1 has proteolytic activity that contributes to optimal NF-jB activation by cleaving the NF-jB inhibitor A20. Whether MALT1 protease activity is involved in other signalling pathways, and the identity of the relevant substrates, is unknown. Here, we show that T-cell receptors (TCR) activation, as well as overexpression of the oncogenic API2-MALT1 fusion protein, results in proteolytic inactivation of CYLD by MALT1, which is specifically required for c-jun N-terminal kinase (JNK) activation and the inducible expression of a subset of genes. These results indicate a novel role for MALT1 proteolytic activity in TCRinduced JNK activation and reveal CYLD cleavage as the underlying mechanism.

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Section: Resultsmentioning

confidence: 99%

T-cell receptor-induced JNK activation requires proteolytic inactivation of CYLD by MALT1

et al. 2011

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“…C‐termini identification methods have been developed during the latest two decades . Among them, some methods involving novel C‐termini enrichment attracted more attention in the proteome‐era .…”

Section: Introductionmentioning

confidence: 99%

An Approach to Incorporate Multi‐Enzyme Digestion into C‐TAILS for C‐Terminomics Studies

Zhang

Huang

et al. 2017

Proteomics

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Protein C-termini study is still a challenging task and far behind its counterpart, N-termini study. MS based C-terminomics study is often hampered by the low ionization efficiency of C-terminal peptides and the lack of efficient enrichment methods. We previously optimized the C-terminal amine-based isotope labeling of substrates (C-TAILS) method and identified 369 genuine protein C-termini in Escherichia coli. A key limitation of C-TAILS is that the prior protection of amines and carboxylic groups at protein level makes Arg-C as the only specific enzyme in practice. Herein, we report an approach combining multi-enzyme digestion and C-TAILS, which significantly increases the identification rate of C-terminal peptides and consequently improves the applicability of C-TAILS in biological studies. We carry out a systematic study and confirm that the omission of the prior amine protection at protein level has a negligible influence and allows the application of multi-enzyme digestion. We successfully apply five different enzyme digestions to C-TAILS, including trypsin, Arg-C, Lys-C, Lys-N, and Lysarginase. As a result, we identify a total of 722 protein C-termini in E. coli, which is at least 66% more than the results using any single enzyme. Moreover, the favored enzyme and enzyme combination are discovered. Data are available via ProteomeXchange with identifier PXD004275.

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“…Probably the simplest and more straightforward strategy to flag C‐terminal peptides in MS spectra is enzymatic 18 O‐labeling . In this strategy, protein digestion is performed in H 2 18 O containing buffer, resulting in the protease‐assisted incorporation of one or two oxygen‐18 atoms at the carboxyl moiety of the hydrolyzed peptide bond, leaving the carboxyl moiety of the original C‐terminal peptide unmodified (Fig.…”

Section: Ms‐based Methods For C‐terminal Sequencing Of Proteinsmentioning

confidence: 99%

“…However, this strategy holds quite some limitations. Given that the rate of cleavage by the CPs strongly depends on the peptide sequence, this method typically requires careful optimization of the reaction conditions, making it overall quite laborious and requiring relatively high amounts of sample .…”

Section: C‐terminal Sequence Analysis: a Historical Perspectivementioning

confidence: 99%

C‐terminomics: Targeted analysis of natural and posttranslationally modified protein and peptide C‐termini

2014

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The C-terminus (where C is carboxyl) of a protein can serve as a recognition signature for a variety of biological processes, including protein trafficking and protein complex formation. Hence, the identity of the in vivo protein C-termini provides valuable information about biological processes. Analysis of protein C-termini is also crucial for the study of C-terminal PTMs, particularly for monitoring proteolytic processing by endopeptidases and carboxypeptidases. Although technical difficulties have limited the study of C-termini, a range of technologies have been proposed in the last couple of years. Here, we review the current proteomics technologies for C-terminal analysis, with a focus on the biological information that can be derived from C-terminomics studies.

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Detection of C-terminal peptide of proteins using isotope coding strategies

Cited by 12 publications

References 25 publications

T-cell receptor-induced JNK activation requires proteolytic inactivation of CYLD by MALT1

T-cell receptor-induced JNK activation requires proteolytic inactivation of CYLD by MALT1

An Approach to Incorporate Multi‐Enzyme Digestion into C‐TAILS for C‐Terminomics Studies

C‐terminomics: Targeted analysis of natural and posttranslationally modified protein and peptide C‐termini

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