CobB1 deacetylase activity in <i>Streptomyces coelicolor</i>

Mikulı́k, Karel; Felsberg, Jürgen; Kudrnáčová, Eva; Bezoušková, Silvia; Šetinová, Dita; Stodůlková, Eva; Zídková, J.; Zidek, Vaclav

doi:10.1139/o11-086

Cited by 34 publications

(41 citation statements)

References 27 publications

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“…lividans encodes two sirtuin deacetylases, CobB1 and CobB2, and a Zn(II)-dependent AcuC-type deacetylase. Work with the closely related organism Streptomyces coelicolor demonstrated that Acs was acetylated and that CobB1 deacetylated Acs in vitro (190). However, the acetyltransferase responsible for the acetylation of S. coelicolor Acs was not identified.…”

Section: Acs From Streptomyces Lividans Is the Exception To The Acs Amentioning

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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Section: Acs From Streptomyces Lividans Is the Exception To The Acs Amentioning

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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“…Around the same time, an investigation of the cobalamin biosynthesis operon in Salmonella led to the discovery of a bacterial sirtuin ortholog, CobB (13), uncovering a bacterial enzyme involved in the regulation of acetylation. CobB was found to regulate acetyl coenzyme A (acetyl-CoA) synthetase (Acs), the second characterized acetylated protein (14)(15)(16)(17)(18)(19)(20)(21)(22)(23). A protein acetyltransferase, Pat, was discovered a few years later in Salmonella (24).…”

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confidence: 99%

Regulation, Function, and Detection of Protein Acetylation in Bacteria

2017

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N -Lysine acetylation is now recognized as an abundant posttranslational modification (PTM) that influences many essential biological pathways. Advancements in mass spectrometry-based proteomics have led to the discovery that bacteria contain hundreds of acetylated proteins, contrary to the prior notion of acetylation events being rare in bacteria. Although the mechanisms that regulate protein acetylation are still not fully defined, it is understood that this modification is finely tuned via both enzymatic and nonenzymatic mechanisms. The opposing actions of Gcn5-related N-acetyltransferases (GNATs) and deacetylases, including sirtuins, provide the enzymatic control of lysine acetylation. A nonenzymatic mechanism of acetylation has also been demonstrated and proven to be prominent in bacteria, as well as in mitochondria. The functional consequences of the vast majority of the identified acetylation sites remain unknown. From studies in mammalian systems, acetylation of critical lysine residues was shown to impact protein function by altering its structure, subcellular localization, and interactions. It is becoming apparent that the same diversity of functions can be found in bacteria. Here, we review current knowledge of the mechanisms and the functional consequences of acetylation in bacteria. Additionally, we discuss the methods available for detecting acetylation sites, including quantitative mass spectrometry-based methods, which promise to promote this field of research. We conclude with possible future directions and broader implications of the study of protein acetylation in bacteria.

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“…The SePat homologue of Streptomyces lividans (SlPatA) has protein acetyltransferase activity that modulates the activity of the acetoacetyl-CoA synthetase enzyme of this bacterium (6). Acetyl-CoA synthetase was also found to be regulated in vivo by acetylation in Streptomyces coelicolor, but the acetyltransferase responsible for this acetylation was not identified (22). The B. subtilis AcuA (211 residues) and Rhodopseudomonas palustris KatA (RpKatA) GNAT enzymes are much smaller than SePat-type acetyltransferases since they contain only the GNAT domain.…”

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confidence: 99%

Acetyl Coenzyme A Synthetase Is Acetylated on Multiple Lysine Residues by a Protein Acetyltransferase with a Single Gcn5-Type N -Acetyltransferase (GNAT) Domain in Saccharopolyspora erythraea

et al. 2014

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bReversible lysine acetylation (RLA) is used by cells of all domains of life to modulate protein function. To date, bacterial acetylation/deacetylation systems have been studied in a few bacteria (e.g., Salmonella enterica, Bacillus subtilis, Escherichia coli, Erwinia amylovora, Mycobacterium tuberculosis, and Geobacillus kaustophilus), but little is known about RLA in antibiotic-producing actinomycetes. Here, we identify the Gcn5-like protein acetyltransferase AcuA of Saccharopolyspora erythraea (SacAcuA, SACE_5148) as the enzyme responsible for the acetylation of the AMP-forming acetyl coenzyme A synthetase (SacAcsA, SACE_2375). Acetylated SacAcsA was deacetylated by a sirtuin-type NAD ؉ -dependent consuming deacetylase (SacSrtN, SACE_3798). In vitro acetylation/deacetylation of SacAcsA enzyme was studied by Western blotting, and acetylation of lysine residues Lys 237 , Lys 380 , Lys 611 , and Lys 628 was confirmed by mass spectrometry. In a strain devoid of SacAcuA, none of the above-mentioned Lys residues of SacAcsA was acetylated. To our knowledge, the ability of SacAcuA to acetylate multiple Lys residues is unique among AcuA-type acetyltransferases. Results from site-specific mutagenesis experiments showed that the activity of SacAcsA was controlled by lysine acetylation. Lastly, immunoprecipitation data showed that in vivo acetylation of SacAcsA was influenced by glucose and acetate availability. These results suggested that reversible acetylation may also be a conserved regulatory posttranslational modification strategy in antibiotic-producing actinomycetes. R eversible lysine acetylation (RLA) of proteins is now recognized as a ubiquitous and conserved posttranslational modification in a variety of organisms (1-4). Recent studies have identified over 2,000 acetylated proteins, ranging from transcriptional factors and ribosomal proteins to metabolic enzymes related to glycolysis, gluconeogenesis, the tricarboxylic acid (TCA) cycle, and fatty acid and nitrogen metabolisms. This kind of posttranslational modification (PTM) has emerged as an important metabolic regulatory mechanism in bacteria since the discovery of acetylation of the Salmonella enterica acetyl coenzyme A (Ac-CoA) synthetase in 2002 (5). In the last decade, lysine acetylation of proteins has been reported in other microorganisms, including Escherichia coli, Bacillus subtilis, Streptomyces lividans, Mycobacterium tuberculosis, Erwinia amylovora, Thermus thermophilus, and Geobacillus kaustophilus (6-9).RLA has been found to modulate protein synthesis, central metabolism, and detoxification metabolism. Yu et al. identified 85 acetylated proteins in E. coli, of which 24 (28%) are involved in protein biosynthesis and 16 (19%) are involved in carbohydrate metabolism (10). Zhang et al. also reported that more than 70% of the 91 acetylated proteins in E. coli are metabolic enzymes (53%) and translation regulators (22%) (11). More recently, Wang et al. identified 235 peptides containing acetylated lysines in a total of 191 proteins in Salmonella ent...

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CobB1 deacetylase activity in Streptomyces coelicolor

Cited by 34 publications

References 27 publications

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

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

Regulation, Function, and Detection of Protein Acetylation in Bacteria

Acetyl Coenzyme A Synthetase Is Acetylated on Multiple Lysine Residues by a Protein Acetyltransferase with a Single Gcn5-Type N -Acetyltransferase (GNAT) Domain in Saccharopolyspora erythraea

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