Autoacetylation of the MYST Lysine Acetyltransferase MOF Protein

Yang, Chao; Wu, Jiang; Sinha, Sarmistha; Neveu, John M.; Zheng, Y. George

doi:10.1074/jbc.m112.359356

Cited by 32 publications

(23 citation statements)

References 36 publications

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“…The majority of HATs have been reported to have autoacetylation, such as p300 (25,26), Rtt109 (27), pCAF (28), human males absent on the first (hMOF) (29,30), yEsa1 (29), and TIP60. Autoacetylation is considered to be an important regulatory model for HATs.…”

Section: Discussionmentioning

confidence: 99%

Regulation of Histone Acetyltransferase TIP60 Function by Histone Deacetylase 3

Huang

Yang

et al. 2014

Journal of Biological Chemistry

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Background: TIP60 can be regulated by autoacetylation and deacetylated by SIRT1. Results: Novel lysine residues of TIP60 autoacetylation were identified, and TIP60 can be functionally regulated by HDAC3 through deacetylation. Conclusion: HDAC3 promotes TIP60 ubiquitination and cytoplasmic localization and protects cells from apoptosis after DNA damage. Significance: Our findings provide a better understanding of TIP60 regulatory mechanisms and its cellular functions.

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Section: Discussionmentioning

confidence: 99%

Regulation of Histone Acetyltransferase TIP60 Function by Histone Deacetylase 3

Huang

Yang

et al. 2014

Journal of Biological Chemistry

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“…Chemical, nonenzymatic lysine acetylation can occur when the pH is Ն8.0 (151,164,165). The autoacetylation activity of some proteins (166) further compounds this problem, leading to reporting of false-positive enzyme-driven acetylation.…”

Section: Bacterial Acetylome Studiesmentioning

confidence: 99%

Acylation of Biomolecules in Prokaryotes: a Widespread Strategy for the Control of Biological Function and Metabolic Stress

Hentchel

Escalante‐Semerena

2015

Microbiol Mol Biol Rev

163

175

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SUMMARY Acylation of biomolecules (e.g., proteins and small molecules) is a process that occurs in cells of all domains of life and has emerged as a critical mechanism for the control of many aspects of cellular physiology, including chromatin maintenance, transcriptional regulation, primary metabolism, cell structure, and likely other cellular processes. Although this review focuses on the use of acetyl moieties to modify a protein or small molecule, it is clear that cells can use many weak organic acids (e.g., short-, medium-, and long-chain mono- and dicarboxylic aliphatics and aromatics) to modify a large suite of targets. Acetylation of biomolecules has been studied for decades within the context of histone-dependent regulation of gene expression and antibiotic resistance. It was not until the early 2000s that the connection between metabolism, physiology, and protein acetylation was reported. This was the first instance of a metabolic enzyme (acetyl coenzyme A [acetyl-CoA] synthetase) whose activity was controlled by acetylation via a regulatory system responsive to physiological cues. The above-mentioned system was comprised of an acyltransferase and a partner deacylase. Given the reversibility of the acylation process, this system is also referred to as r eversible l ysine a cylation (RLA). A wealth of information has been obtained since the discovery of RLA in prokaryotes, and we are just beginning to visualize the extent of the impact that this regulatory system has on cell function.

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“…Numerous examples of autocatalytic activation have been described for kinases and phosphatases, but only very few cases are known in which acetyltransferases or protein deacetylases undergo activation by autoacetylation or autodeacetylation [25–28]. Recently, we defined an autodeacetylation activity for Sirt1, which is inhibited by Sirt7.…”

Section: Discussionmentioning

confidence: 99%

Sirt7 inhibits Sirt1-mediated activation of Suv39h1

et al. 2018

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Sirtuins regulate a variety of cellular processes through protein deacetylation. The best-known member of mammalian sirtuin family, Sirt1, plays important roles in the maintenance of cellular homeostasis by regulating cell metabolism, differentiation and stress responses, among others. Sirt1 activity requires tight regulation to meet specific cellular requirements, which is achieved at different levels and by specific mechanisms. Recently, a regulatory loop between Sirt1 and another sirtuin, Sirt7, was identified. Sirt7 inhibits Sirt1 autodeacetylation at K230 and activation thereby preventing Sirt1-mediated repression of adipocyte differentiation by inhibition of the PPARγ gene. Here, we extend the regulatory complexity of Sirt7-dependent restriction of Sirt1 activity by demonstrating that Sirt7 reduces activation of a previously described prominent Sirt1 target, the histone methyltransferase Suv39h1. We show that removal of the acetyl-group at K230 in Sirt1 due to the absence of Sirt7 leads to hyperactivation of Sirt1 and thereby to constantly increased activity of Suv39h1.

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Autoacetylation of the MYST Lysine Acetyltransferase MOF Protein

Cited by 32 publications

References 36 publications

Regulation of Histone Acetyltransferase TIP60 Function by Histone Deacetylase 3

Regulation of Histone Acetyltransferase TIP60 Function by Histone Deacetylase 3

Acylation of Biomolecules in Prokaryotes: a Widespread Strategy for the Control of Biological Function and Metabolic Stress

Sirt7 inhibits Sirt1-mediated activation of Suv39h1

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