Identification of Novel Protein Lysine Acetyltransferases in Escherichia coli

Christensen, David G.; Meyer, Jesse G.; Baumgartner, Jackson; D’Souza, Alexandria K.; Nelson, Karen E.; Payne, Samuel H.; Kuhn, Misty L.; Schilling, Birgit; Wolfe, Alan J.

doi:10.1128/mbio.01905-18

Cited by 98 publications

(139 citation statements)

References 81 publications

(109 reference statements)

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“…Furthermore, a number of expression systems have been devised in E. coli to deliver proteins with intact acetylation patterns. For example, E. coli is known to harbor multiple endogenous N ε -lysine acetyltransferases (KATs), which catalyzes acetylation of lysine side chains embedded within proteins [66]. It was demonstrated that the native acetylation machineries in E. coli can be exploited to effectively acetylate human thymosin α1, suggesting that production of acetylated proteins is likely achievable in recombinant microbes ( Figure 1A and Table 1) [47].…”

Section: Engineered E Coli For Wide Array Of Recombinant Proteinsmentioning

confidence: 99%

Engineering Biology to Construct Microbial Chassis for the Production of Difficult-to-Express Proteins

Kim

Choe

Lee

et al. 2020

IJMS

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A large proportion of the recombinant proteins manufactured today rely on microbe-based expression systems owing to their relatively simple and cost-effective production schemes. However, several issues in microbial protein expression, including formation of insoluble aggregates, low protein yield, and cell death are still highly recursive and tricky to optimize. These obstacles are usually rooted in the metabolic capacity of the expression host, limitation of cellular translational machineries, or genetic instability. To this end, several microbial strains having precisely designed genomes have been suggested as a way around the recurrent problems in recombinant protein expression. Already, a growing number of prokaryotic chassis strains have been genome-streamlined to attain superior cellular fitness, recombinant protein yield, and stability of the exogenous expression pathways. In this review, we outline challenges associated with heterologous protein expression, some examples of microbial chassis engineered for the production of recombinant proteins, and emerging tools to optimize the expression of heterologous proteins. In particular, we discuss the synthetic biology approaches to design and build and test genome-reduced microbial chassis that carry desirable characteristics for heterologous protein expression.

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Section: Engineered E Coli For Wide Array Of Recombinant Proteinsmentioning

confidence: 99%

Engineering Biology to Construct Microbial Chassis for the Production of Difficult-to-Express Proteins

Kim

Choe

Lee

et al. 2020

IJMS

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“…Additional substrates for E. coli YfiQ (EcYfiQ) have also been identified, expanding the number of known protein substrates and potential regulatory roles for this enzyme (76). The oligomeric state of S.…”

Section: Introductionmentioning

confidence: 99%

“…Recently, four new type IV GNATs from E. coli were identified (YiaC, YjaB, RimI, and PhnO), and they appear to acetylate a wide range of protein substrates (76). Previously, the M.…”

Section: Introductionmentioning

confidence: 99%

Mechanisms, Detection, and Relevance of Protein Acetylation in Prokaryotes

Christensen

Baumgartner

Xie

et al. 2019

mBio

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115

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Posttranslational modification of a protein, either alone or in combination with other modifications, can control properties of that protein, such as enzymatic activity, localization, stability, or interactions with other molecules. N-ε-Lysine acetylation is one such modification that has gained attention in recent years, with a prevalence and significance that rival those of phosphorylation. This review will discuss the current state of the field in bacteria and some of the work in archaea, focusing on both mechanisms of N-ε-lysine acetylation and methods to identify, quantify, and characterize specific acetyllysines. Bacterial N-ε-lysine acetylation depends on both enzymatic and nonenzymatic mechanisms of acetylation, and recent work has shed light into the regulation of both mechanisms. Technological advances in mass spectrometry have allowed researchers to gain insight with greater biological context by both (i) analyzing samples either with stable isotope labeling workflows or using label-free protocols and (ii) determining the true extent of acetylation on a protein population through stoichiometry measurements. Identification of acetylated lysines through these methods has led to studies that probe the biological significance of acetylation. General and diverse approaches used to determine the effect of acetylation on a specific lysine will be covered.

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“…In E. coli two distinct mechanisms are responsible for Nε‐lysine acetylation. The Nε‐lysine acetyltransferases, such as the best characterized YfiQ (also known as PatZ or Pka) and the recently discovered RimI, YiaC, YjaB and PhnO catalyze acetylation of specific lysines using acetyl‐CoA as the acetyl donor (Christensen et al , ). An alternative non‐enzymatic mechanism involves acetyl phosphate and is a dominant form of acetylation in E. coli.…”

Section: Introductionmentioning

confidence: 99%

Trehalose protects Escherichia coli against carbon stress manifested by protein acetylation and aggregation

Algara

Kuczyńska-Wiśnik

Dębski

et al. 2019

Molecular Microbiology

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Summary The disaccharide trehalose is widely distributed in nature and can serve as a carbon reservoir, a signaling molecule for controlling glucose metabolism and a stress protectant. We demonstrated that in Escherichia coli ΔotsA cells, which are unable to synthesize trehalose, the aggregation of endogenous proteins during the stationary phase was increased in comparison to wild‐type cells. The lack of trehalose synthesis boosted Nε‐lysine acetylation of proteins, which in turn enhanced their hydrophobicity and aggregation. This increased Nε‐lysine acetylation could result from carbon overflow and the accumulation of acetyl phosphate caused by the ΔotsA mutation. These findings provide a better understanding of the previously reported protective functions of trehalose in protein stabilization and the prevention of protein aggregation. Our results indicate that trehalose may participate in proteostasis not only as a chemical chaperone but also as a metabolite that indirectly counteracts detrimental protein acetylation. We propose that trehalose protects E. coli against carbon stress – the synthesis and storage of trehalose can prevent carbon overflow, which otherwise is manifested by protein acetylation and aggregation.

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Identification of Novel Protein Lysine Acetyltransferases in Escherichia coli

Cited by 98 publications

References 81 publications

Engineering Biology to Construct Microbial Chassis for the Production of Difficult-to-Express Proteins

Engineering Biology to Construct Microbial Chassis for the Production of Difficult-to-Express Proteins

Mechanisms, Detection, and Relevance of Protein Acetylation in Prokaryotes

Trehalose protects Escherichia coli against carbon stress manifested by protein acetylation and aggregation

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