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The 20S Proteasome Splicing Activity Discovered by SpliceMet

Liepe, J; Mishto, M; Textoris-Taube, K; Janek, K; Keller, C; Henklein, P; Kloetzel, PM; (2010) The 20S Proteasome Splicing Activity Discovered by SpliceMet. PLoS Computational Biology , 6 (6) , Article e1000830. 10.1371/journal.pcbi.1000830. Green open access

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Abstract

The identification of proteasome-generated spliced peptides (PSP) revealed a new unpredicted activity of the major cellular protease. However, so far characterization of PSP was entirely dependent on the availability of patient-derived cytotoxic CD8+ T lymphocytes (CTL) thus preventing a systematic investigation of proteasome-catalyzed peptide splicing (PCPS). For an unrestricted PSP identification we here developed SpliceMet, combining the computer-based algorithm ProteaJ with in vitro proteasomal degradation assays and mass spectrometry. By applying SpliceMet for the analysis of proteasomal processing products of four different substrate polypeptides, derived from human tumor as well as viral antigens, we identified fifteen new spliced peptides generated by PCPS either by cis or from two separate substrate molecules, i.e., by trans splicing. Our data suggest that 20S proteasomes represent a molecular machine that, due to its catalytic and structural properties, facilitates the generation of spliced peptides, thereby providing a pool of qualitatively new peptides from which functionally relevant products may be selected.

Type: Article
Title: The 20S Proteasome Splicing Activity Discovered by SpliceMet
Open access status: An open access version is available from UCL Discovery
DOI: 10.1371/journal.pcbi.1000830
Publisher version: http://dx.doi.org/10.1371/journal.pcbi.1000830
Language: English
Additional information: © 2010 Liepe et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
Keywords: PROTEOME ANALYSIS, ANTIGEN, EPITOPE, DEGRADATION, PEPTIDES, COMPLEX, TRANSPEPTIDATION, RECOGNITION, GENERATION, SEQUENCE
UCL classification: UCL
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Population Health Sciences > UCL EGA Institute for Womens Health
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Population Health Sciences > UCL EGA Institute for Womens Health > Womens Cancer
URI: https://discovery.ucl.ac.uk/id/eprint/142396
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