Improved Mass Spectrometry-Based Methods Reveal Abundant Propionylation and Tissue-Specific Histone Propionylation Profiles.

Autor:	Vai A; Department of Experimental Oncology, European Institute of Oncology (IEO) IRCSS, Milan, Italy., Noberini R; Department of Experimental Oncology, European Institute of Oncology (IEO) IRCSS, Milan, Italy., Ghirardi C; Department of Experimental Oncology, European Institute of Oncology (IEO) IRCSS, Milan, Italy., Rodrigues de Paula D; International Laboratory for Microbiome Host Epigenetics, Department of Genetics, Evolution, Microbiology, and Immunology, Institute of Biology, University of Campinas, Campinas, São Paulo, Brazil., Carminati M; Department of Experimental Oncology, European Institute of Oncology (IEO) IRCSS, Milan, Italy., Pallavi R; Department of Experimental Oncology, European Institute of Oncology (IEO) IRCSS, Milan, Italy., Araújo N; International Laboratory for Microbiome Host Epigenetics, Department of Genetics, Evolution, Microbiology, and Immunology, Institute of Biology, University of Campinas, Campinas, São Paulo, Brazil., Varga-Weisz P; International Laboratory for Microbiome Host Epigenetics, Department of Genetics, Evolution, Microbiology, and Immunology, Institute of Biology, University of Campinas, Campinas, São Paulo, Brazil; São Paulo Excellence Chair, Department of Genetics, Evolution, Microbiology, and Immunology, Institute of Biology, University of Campinas, Campinas, São Paulo, Brazil; School of Biological Sciences, University of Essex, Colchester, UK., Bonaldi T; Department of Experimental Oncology, European Institute of Oncology (IEO) IRCSS, Milan, Italy; Department of Oncology and Hematology-Oncology (DIPO), University of Milan, Milan, Italy. Electronic address: tiziana.bonaldi@ieo.it.
Jazyk:	angličtina
Zdroj:	Molecular & cellular proteomics : MCP [Mol Cell Proteomics] 2024 Jul; Vol. 23 (7), pp. 100799. Date of Electronic Publication: 2024 Jun 11.
DOI:	10.1016/j.mcpro.2024.100799
Abstrakt:	Histone posttranslational modifications (PTMs) have crucial roles in a multitude of cellular processes, and their aberrant levels have been linked with numerous diseases, including cancer. Although histone PTM investigations have focused so far on methylations and acetylations, alternative long-chain acylations emerged as new dimension, as they are linked to cellular metabolic states and affect gene expression through mechanisms distinct from those regulated by acetylation. Mass spectrometry is the most powerful, comprehensive, and unbiased method to study histone PTMs. However, typical mass spectrometry-based protocols for histone PTM analysis do not allow the identification of naturally occurring propionylation and butyrylation. Here, we present improved state-of-the-art sample preparation and analysis protocols to quantitate these classes of modifications. After testing different derivatization methods coupled to protease digestion, we profiled common histone PTMs and histone acylations in seven mouse tissues and human normal and tumor breast clinical samples, obtaining a map of propionylations and butyrylations found in different tissue contexts. A quantitative histone PTM analysis also revealed a contribution of histone acylations in discriminating different tissues, also upon perturbation with antibiotics, and breast cancer samples from the normal counterpart. Our results show that profiling only classical modifications is limiting and highlight the importance of using sample preparation methods that allow the analysis of the widest possible spectrum of histone modifications, paving the way for deeper insights into their functional significance in cellular processes and disease states. Competing Interests: Conflicts of interest A. V. and M. C. are PhD students within the European School of Molecular Medicine (SEMM). The other authors declare no competing interests. (Copyright © 2024 The Authors. Published by Elsevier Inc. All rights reserved.)
Databáze:	MEDLINE
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