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O-GlcNAcylation stimulates the deubiquitination activity of USP16 and regulates cell cycle progression.
J Biol Chem
April 2024
Beijing Key Laboratory of DNA Damage Response and College of Life Science, Capital Normal University, Beijing, China. Electronic address:
Histone 2A monoubiquitination (uH2A) underscores a key epigenetic regulation of gene expression. In this report, we show that the deubiquitinase for uH2A, ubiquitin-specific peptidase 16 (USP16), is modified by O-linked N-acetylglucosamine (O-GlcNAc). O-GlcNAcylation involves the installation of the O-GlcNAc moiety to Ser/Thr residues.
View Article and Find Full Text PDFBiocompatible Lysine Protecting Groups for the Chemoenzymatic Synthesis of K48/K63 Heterotypic and Branched Ubiquitin Chains.
ACS Cent Sci
August 2023
Laboratory for Organic Chemistry, Department of Chemistry and Applied Biosciences, ETH Zürich, Vladimir-Prelog-Weg 3, CH-8093 Zürich, Switzerland.
The elucidation of emerging biological functions of heterotypic and branched ubiquitin (Ub) chains requires new strategies for their preparation with defined lengths and connectivity. While enzymatic assembly using expressed E1-activating and E2-conjugating enzymes can deliver homotypic chains, the synthesis of branched chains typically requires extensive mutations of lysines or other sequence modifications. The combination of K48- and K63-biased E2-conjugating enzymes and two new carbamate protecting groups-pyridoxal 5'-phosphate (PLP)-cleavable aminobutanamide carbamate (Abac group) and periodate-cleavable aminobutanol carbamate (Aboc group)-provides a strategy for the synthesis of heterotypic and branched Ub trimers, tetramers, and pentamers.
View Article and Find Full Text PDFOne-Step Sortase-Mediated Chemoenzymatic Semisynthesis of Deubiquitinase-Resistant Ub-Peptide Conjugates.
ACS Omega
December 2022
Department of Chemical Biology, Faculty of Biotechnology, University of Wrocław, F. Joliot-Curie 14a, 50-383 Wrocław, Poland.
Post-translational modifications (PTMs) of proteins increase the functional diversity of the proteome and play crucial regulatory roles in cellular processes. Ubiquitination is a highly regulated and reversible PTM accomplished by a complex multistep process with the sequential action of several specific ubiquitinating (E1-E3) and deubiquitinating enzymes. The different types of ubiquitination (mono-, poly-mono-, and poly-) and the presence of several target sites in a single substrate add to its complexity, which makes the in vitro reconstitution of this ubiquitin (Ub) machinery a quite cumbersome process.
View Article and Find Full Text PDFExpedient Synthesis of Ubiquitin-like Protein ISG15 Tools through Chemo-Enzymatic Ligation Catalyzed by a Viral Protease Lb.
Angew Chem Int Ed Engl
October 2022
Department of Chemistry, Key Laboratory of Bioorganic Phosphorus Chemistry & Chemical Biology, Tsinghua University, Beijing, 100084, P. R. China.
Ubiquitin (Ub)-like protein ISG15 (interferon-stimulated gene 15) regulates innate immunity and links with the evasion of host response by viruses such as SARS-CoV-2. Dissecting ISGylation pathways recently received increasing attention which can inform related disease interventions, but such studies necessitate the preparation and development of various ISG15 protein tools. Here, we find that the leader protease (Lb ) encoded by foot-and-mouth disease virus can promote ligation reactions between recombinant ISG15 and synthetic glycyl compounds, generating protein tools such as ISG15-propargylamide and ISG15-rhodamine110, which are needed for cellular proteomic studies of deISGylases, and the screening and evaluation of inhibitors against SARS-CoV-2 papain-like protease (PLpro).
View Article and Find Full Text PDFAdvances in enrichment methods for mass spectrometry-based proteomics analysis of post-translational modifications.
J Chromatogr A
August 2022
Department of Biotechnology, University of Verona, Strada le Grazie 15, 37134 Verona, Italy. Electronic address:
Article Synopsis
- - Post-translational modifications (PTMs) enhance protein diversity and affect various cellular functions, with key types including phosphorylation, acetylation, and glycosylation among others.
- - Mass-spectrometry (MS) is the leading technique for analyzing PTMs, but the process is complicated due to the low abundance and unstable nature of modified peptides, necessitating methods for peptide enrichment before analysis.
- - The review covers traditional enrichment techniques like immunoenrichment and chromatography, as well as newer chemical strategies, highlighting their advantages and limitations, and discusses ongoing challenges and future directions in the study of PTMs.
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