A genetically encoded <sup>19</sup>F NMR probe for lysine acetylation

Zhang, Feng; Zhou, Qing; Yang, Guangming; An, Liguo; Li, Fahui; Wang, Jiangyun

doi:10.1039/c7cc09825a

Cited by 44 publications

(49 citation statements)

References 43 publications

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“…[13–14] Fluorine is absent from any naturally occurring biological molecule, yet it can be readily and selectively incorporated into proteins, [15–17] largely without causing major structural perturbations. [18] 19 F NMR, both solution and solid-state, has therefore emerged as an essential method with broad applications in pharmaceutical chemistry (as ~30% of all drugs at present in the clinic contain fluorine), [19] chemical biology, [20] biochemistry, [16, 21–24] and materials science. [25] 19 F NMR has been applied to investigate proteins, lipids, nucleic acids, synthetic small-molecule ligands, as well as their complexes, both in solution [16, 21] and in the solid state.…”

mentioning

confidence: 99%

Fast Magic‐Angle Spinning ¹⁹F NMR Spectroscopy of HIV‐1 Capsid Protein Assemblies

Wang

Fritz

et al. 2018

Angew Chem Int Ed

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F NMR spectroscopy is an attractive and growing area of research with broad applications in biochemistry, chemical biology, medicinal chemistry, and materials science. We have explored fast magic angle spinning (MAS) F solid-state NMR spectroscopy in assemblies of HIV-1 capsid protein. Tryptophan residues with fluorine substitution at the 5-position of the indole ring were used as the reporters. The F chemical shifts for the five tryptophan residues are distinct, reflecting differences in their local environment. Spin-diffusion and radio-frequency-driven-recoupling experiments were performed at MAS frequencies of 35 kHz and 40-60 kHz, respectively. Fast MAS frequencies of 40-60 kHz are essential for consistently establishing F- F correlations, yielding interatomic distances of the order of 20 Å. Our results demonstrate the potential of fast MAS F NMR spectroscopy for structural analysis in large biological assemblies.

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confidence: 99%

Fast Magic‐Angle Spinning ¹⁹F NMR Spectroscopy of HIV‐1 Capsid Protein Assemblies

Wang

Fritz

et al. 2018

Angew Chem Int Ed

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“…Non‐hydrolysable analogues of acetyl‐lysine that prevent the turnover of the modification have been developed and incorporated in proteins in E. coli . [ 30 – 32 ] These analogues have immense potential in revealing the physiological role of lysine acetylation.…”

Section: Gce Strategies To Produce Site‐specifically and Quantitatively Acylated Proteinsmentioning

confidence: 99%

Genetic Code Expansion Tools to Study Lysine Acylation

Neumann‐Staubitz¹,

Lammers

Neumann³

2021

Advanced Biology

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Lysine acylation is a ubiquitous protein modification that controls various aspects of protein function, such as the activity, localization, and stability of enzymes. Mass spectrometric identification of lysine acylations has witnessed tremendous improvements in sensitivity over the last decade, facilitating the discovery of thousands of lysine acylation sites in proteins involved in all essential cellular functions across organisms of all domains of life. However, the vast majority of currently known acylation sites are of unknown function. Semi‐synthetic methods for installing lysine derivatives are ideally suited for in vitro experiments, while genetic code expansion (GCE) allows the installation and study of such lysine modifications, especially their dynamic properties, in vivo. An overview of the current state of the art is provided, and its potential is illustrated with case studies from recent literature. These include the application of engineered enzymes and GCE to install lysine modifications or photoactivatable crosslinker amino acids. Their use in the context of central metabolism, bacterial and viral pathogenicity, the cytoskeleton and chromatin dynamics, is investigated.

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“…Very recently, Zhang et al genetically incorporated trifluoro-acetyllysine (TFAcK) into p53 to detect the conformational changes by NMR (nuclear magnetic resonance). They also demonstrated that the TFAcK-containing p53 protein could not be deacetylated by sirtuin deacetylase [ 46 ].…”

Section: Lysine Acetylation and Its Analogs By Genetic Code Expansmentioning

confidence: 99%

Recent Development of Genetic Code Expansion for Posttranslational Modification Studies

et al. 2018

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Nowadays advanced mass spectrometry techniques make the identification of protein posttranslational modifications (PTMs) much easier than ever before. A series of proteomic studies have demonstrated that large numbers of proteins in cells are modified by phosphorylation, acetylation and many other types of PTMs. However, only limited studies have been performed to validate or characterize those identified modification targets, mostly because PTMs are very dynamic, undergoing large changes in different growth stages or conditions. To overcome this issue, the genetic code expansion strategy has been introduced into PTM studies to genetically incorporate modified amino acids directly into desired positions of target proteins. Without using modifying enzymes, the genetic code expansion strategy could generate homogeneously modified proteins, thus providing powerful tools for PTM studies. In this review, we summarized recent development of genetic code expansion in PTM studies for research groups in this field.

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A genetically encoded ¹⁹F NMR probe for lysine acetylation

Cited by 44 publications

References 43 publications

Fast Magic‐Angle Spinning ¹⁹F NMR Spectroscopy of HIV‐1 Capsid Protein Assemblies

Fast Magic‐Angle Spinning ¹⁹F NMR Spectroscopy of HIV‐1 Capsid Protein Assemblies

Genetic Code Expansion Tools to Study Lysine Acylation

Recent Development of Genetic Code Expansion for Posttranslational Modification Studies

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A genetically encoded 19F NMR probe for lysine acetylation

Cited by 44 publications

References 43 publications

Fast Magic‐Angle Spinning 19F NMR Spectroscopy of HIV‐1 Capsid Protein Assemblies

Fast Magic‐Angle Spinning 19F NMR Spectroscopy of HIV‐1 Capsid Protein Assemblies

Genetic Code Expansion Tools to Study Lysine Acylation

Recent Development of Genetic Code Expansion for Posttranslational Modification Studies

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A genetically encoded ¹⁹F NMR probe for lysine acetylation

Fast Magic‐Angle Spinning ¹⁹F NMR Spectroscopy of HIV‐1 Capsid Protein Assemblies

Fast Magic‐Angle Spinning ¹⁹F NMR Spectroscopy of HIV‐1 Capsid Protein Assemblies