Lysine Propionylation and Butyrylation Are Novel Post-translational Modifications in Histones*S

By Yue Chen, R. Sprung, Yi Tang, H. Ball, Bhavani Sangras, S. Kim, J. Falck, Junmin Peng, W. Gu, Yingming Zhao. Molecular & Cellular Proteomics, 2007

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The positively charged lysine residue plays an important role in protein folding and functions. Neutralization of the charge often has a profound impact on the substrate proteins. Accordingly all the known post-translational modifications at lysine have pivotal roles in cell physiology and pathology. Here we report the discovery of two novel, in vivo lysine modifications in histones, lysine propionylation and butyrylation. We confirmed, by in vitro labeling and peptide mapping by mass spectrometry, that two previously known acetyltransferases, p300 and CREB-binding protein, could catalyze lysine propionylation and lysine butyrylation in histones. Finally p300 and CREB-binding protein could carry out autopropionylation and autobutyrylation in vitro. Taken together, our results conclusively establish that lysine propionylation and lysine butyrylation are novel post-translational modifications. Given the unique roles of propionyl-CoA and butyryl-CoA in energy metabolism and the significant structural changes induced by the modifications, the two modifications are likely to have important but distinct functions in the regulation of biological processes.

Subfields: Geriatrics and Gerontology, Molecular Biology, Oncology

View Paper: https://www.semanticscholar.org/paper/18a01720e6f78786a82fa10698c15617e60c8301

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Citations in the corpus

Histone Modifications and Cancer. (2016, neutral): “…citrullination, ubiquitination, ADP-ribosylation, deamination, formylation, O-GlcNAcylation, propionylation, butyrylation, crotonylation, and proline isomerization (Chen et al. 2007; Martin and Zhang 2007; Ruthenburg et al. 2007; Tan et al. 2011; Herranz et al. 2012; Tweedie-Cullen et al. 2012).”
Identification of lysine succinylation as a new post-translational modification (2010, background): “Lysine residues in proteins can be subjected to a variety of PTMs, including methylation, acetylation, biotinylation, ubiquitination, ubiquitin-like modifications, propionylation and butyrylation, the last two of which were recently identified by u”
Interpreting thelanguage of histone and DNA modifications (2014, background): “For example, what are the writers, erasers, and potential readers of these modifications? In the case of lysine butyrylation and propionylation, which use distinct co-enzyme A cofactors (butyryl-CoA and propionyl-CoA), studies have shown that they can be catalyzed and removed by histone acetyltransf”
Lysine Glutarylation Is a Protein Post-Translational Modification Regulated by SIRT5 (2014, background): “Our previous studies identified new lysine acylation modifications on histones (Chen et al., 2007; Tan et al., 2011; Xie et al., 2012), including lysine crotonylation and succinylation, revealing potential crosstalk between cellular physiology and gene transcription.”
HATs and HDACs: from structure, function and regulation to novel strategies for therapy and prevention (2007, background): “These enzymes may also control lysine acetylationlike modifications, such as propioylation and butyrylation (Chen et al., 2007).”
The world of protein acetylation. (2016, background): “Thereby, they are able to autopropionylate someof their own lysine residues [175].”
Lysine succinylation is a frequently occurring modification in prokaryotes and eukaryotes and extensively overlaps with acetylation. (2013, background): “, 2011), propionylation (Chen et al., 2007), butyrylation (Chen et al.”
SIRT5-Mediated Lysine Desuccinylation Impacts Diverse Metabolic Pathways (2013, background): “…of numerous PTMs; e.g., acetylation, methylation, biotinylation, ubiquitination and ubiquitin-likemodifications, butyrylation, propionylation, crotonylation, malonylation, and succinylation (Berger, 2007; Chen et al., 2007; Peng et al., 2011; Tan et al., 2011; Xie et al., 2012; Zhang et al., 2011).”