HBO1 catalyzes lysine benzoylation in mammalian cells

Tan, Doudou; Wei, Wei; Han, Zhigang; Ren, Xuelian; Qi, Shankang; Song, Xiaohan; Zheng, Y. George; Wong, Jiemin; Huang, He

doi:10.1016/j.isci.2022.105443

Cited by 17 publications

(18 citation statements)

References 34 publications

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“… 1439 Previous studies have showed that HBO1 and the Spt‐Ada‐Gcn5 acetyltransferase complex are writers of histone Kbz. 1440 , 1441 In vivo studies have found that SIRT2, unlike other sirtuins or histone deacetylases (HDACs), acts as an eraser of histone Kbz. 1436 NAD + ‐dependent histone deacetylase Hst2 has debenzoylase activity in yeast.…”

Section: Other Modificationsmentioning

confidence: 99%

“…Moreover, benzoyl‐CoA is also a central intermediate for the degradation of numerous aromatic growth substrates in bacteria and gut microbes 1439 . Previous studies have showed that HBO1 and the Spt‐Ada‐Gcn5 acetyltransferase complex are writers of histone Kbz 1440,1441 . In vivo studies have found that SIRT2, unlike other sirtuins or histone deacetylases (HDACs), acts as an eraser of histone Kbz 1436 .…”

Section: Other Modificationsmentioning

confidence: 99%

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Protein posttranslational modifications in health and diseases: Functions, regulatory mechanisms, and therapeutic implications

Zhong

Xiao

Xie

et al. 2023

MedComm

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Protein posttranslational modifications (PTMs) refer to the breaking or generation of covalent bonds on the backbones or amino acid side chains of proteins and expand the diversity of proteins, which provides the basis for the emergence of organismal complexity. To date, more than 650 types of protein modifications, such as the most well‐known phosphorylation, ubiquitination, glycosylation, methylation, SUMOylation, short‐chain and long‐chain acylation modifications, redox modifications, and irreversible modifications, have been described, and the inventory is still increasing. By changing the protein conformation, localization, activity, stability, charges, and interactions with other biomolecules, PTMs ultimately alter the phenotypes and biological processes of cells. The homeostasis of protein modifications is important to human health. Abnormal PTMs may cause changes in protein properties and loss of protein functions, which are closely related to the occurrence and development of various diseases. In this review, we systematically introduce the characteristics, regulatory mechanisms, and functions of various PTMs in health and diseases. In addition, the therapeutic prospects in various diseases by targeting PTMs and associated regulatory enzymes are also summarized. This work will deepen the understanding of protein modifications in health and diseases and promote the discovery of diagnostic and prognostic markers and drug targets for diseases.

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Section: Other Modificationsmentioning

confidence: 99%

Section: Other Modificationsmentioning

confidence: 99%

Protein posttranslational modifications in health and diseases: Functions, regulatory mechanisms, and therapeutic implications

Zhong

Xiao

Xie

et al. 2023

MedComm

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“…In addition to modification on the core histones, Kbz and Kinic also modify non‐histone proteins. Over 1,700 Kbz sites on cellular proteins in mammalian cells were discovered (D. Tan et al., 2022). Kbz marks formed by HBO1, a reported ‘writer’ of Kbz in mammalian cells, have been reported to be involved in multiple critical processes such as transcription regulation, chromatin remodeling, tumor growth, and immune regulation (D. Tan et al., 2022).…”

Section: Overview Of New Lysine Acylation Biomarkersmentioning

confidence: 99%

“…Over 1,700 Kbz sites on cellular proteins in mammalian cells were discovered (D. Tan et al., 2022). Kbz marks formed by HBO1, a reported ‘writer’ of Kbz in mammalian cells, have been reported to be involved in multiple critical processes such as transcription regulation, chromatin remodeling, tumor growth, and immune regulation (D. Tan et al., 2022). In yeast, Kbz‐modified non‐histone proteins are enriched in glycolysis/gluconeogenesis, ribosome biogenesis, and rRNA processing pathways (D. Wang et al., 2022).…”

Section: Overview Of New Lysine Acylation Biomarkersmentioning

confidence: 99%

“…In yeast, Kbz‐modified non‐histone proteins are enriched in glycolysis/gluconeogenesis, ribosome biogenesis, and rRNA processing pathways (D. Wang et al., 2022). Excessive intake of SB can increase the risk of diseases, including ADHD symptoms and motor coordination impairment (D. Tan et al., 2022). In terms of the role of Kinic on non‐histone proteins, another study demonstrated the high association of INH‐induced Kinic with certain types of cancer (Y. Jiang et al., 2021).…”

Section: Overview Of New Lysine Acylation Biomarkersmentioning

confidence: 99%

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New Histone Lysine Acylation Biomarkers and Their Roles in Epigenetic Regulation

Cat

Zheng

2023

Current Protocols

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Protein posttranslational modification (PTM) is a biochemical mechanism benefitting cellular adaptation to dynamic intracellular and environmental conditions. Recently, several acylation marks have been identified as new protein PTMs occurring on specific lysine residues in mammalian cells: isobutyrylation, methacrylation, benzoylation, isonicotinylation, and lactylation. These acylation marks were initially discovered to occur on nucleosomal histones, but they potentially occur as prevalent biomarkers on non-histone proteins as well. The existence of these PTMs is a downstream consequence of metabolism and demonstrates the intimate crosstalk between active cellular metabolites and regulation of protein function. Emerging evidence indicates that these acylation marks on histones affect DNA transcription and are functionally distinct from the well-studied lysine acetylation. Herein, we discuss enzymatic regulation and metabolic etiology of these acylations, 'reader' proteins that recognize different acylations, and their possible physiological and pathological functions. Several of these modifications correlate with other well-studied acylations and fine-tune the regulation of gene expression. Overall, findings of these acylation marks reveal new molecular links between metabolism and epigenetics and open up many questions for future investigation.

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Promiscuous Enzymes for Residue‐Specific Peptide and Protein Late‐Stage Functionalization

Alexander

Elshahawi

2023

ChemBioChem

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The late‐stage functionalization of peptides and proteins holds significant promise for drug discovery and facilitates bioorthogonal chemistry. This selective functionalization leads to innovative advances in in vitro and in vivo biological research. However, it is a challenging endeavor to selectively target a certain amino acid or position in the presence of other residues containing reactive groups. Biocatalysis has emerged as a powerful tool for selective, efficient, and economical modifications of molecules. Enzymes that have the ability to modify multiple complex substrates or selectively install nonnative handles have wide applications. Herein, we highlight enzymes with broad substrate tolerance that have been demonstrated to modify a specific amino acid residue in simple or complex peptides and/or proteins at late‐stage. The different substrates accepted by these enzymes are mentioned together with the reported downstream bioorthogonal reactions that have benefited from the enzymatic selective modifications.

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HBO1 catalyzes lysine benzoylation in mammalian cells

Cited by 17 publications

References 34 publications

Protein posttranslational modifications in health and diseases: Functions, regulatory mechanisms, and therapeutic implications

Protein posttranslational modifications in health and diseases: Functions, regulatory mechanisms, and therapeutic implications

New Histone Lysine Acylation Biomarkers and Their Roles in Epigenetic Regulation

Promiscuous Enzymes for Residue‐Specific Peptide and Protein Late‐Stage Functionalization

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