Site-specific determination of lysine acetylation stoichiometries on the proteome-scale

2019 ◽  
pp. 115-132
Author(s):  
Yue Chen ◽  
Yunan Li
Keyword(s):  
Lysine Acetylation ◽  
Site Specific ◽  
Specific Determination

scholarly journals Combined Metabolic and Chemical (CoMetChem) Labeling Using Stable Isotopes – a Strategy to Reveal Site-Specific Histone Acetylation and Deacetylation Rates by LC-MS

2021 ◽  
Author(s):  
Alienke van Pijkeren ◽  
Jörn Dietze ◽  
Alejandro Sánchez Brotons ◽  
Tim Lijster ◽  
Andrei Barcaru ◽  
...  
Keyword(s):  
Histone Acetylation ◽  
Protein Modification ◽  
High Resolution Mass Spectrometry ◽  
Reaction Rates ◽  
Lysine Acetylation ◽  
Chemical Labeling ◽  
Comprehensive Description ◽  
Site Specific ◽  
New Approach

Histone acetylation is an important, reversible post-translational protein modification and a hallmark of epigenetic regulation. However, little is known about the dynamics of this process, due to the lack of analytical methods that can capture site-specific acetylation and deacetylation reactions. We present a new approach that combines metabolic and chemical labeling (CoMetChem) using uniformly 13C-labeled glucose and stable isotope labeled acetic anhydride. Thereby, chemically equivalent, fully acetylated histone species are generated enabling accurate relative quantification of site-specific lysine acetylation in tryptic peptides using high-resolution mass spectrometry. We show that CoMetChem enables site-specific quantification of the incorporation or loss of lysine acetylation over time, allowing the determination of reaction rates for acetylation and deacetylation. Thus, the CoMetChem methodology provides a comprehensive description of site-specific acetylation dynamics. <br>

scholarly journals Combined Metabolic and Chemical (CoMetChem) Labeling Using Stable Isotopes – a Strategy to Reveal Site-Specific Histone Acetylation and Deacetylation Rates by LC-MS

2021 ◽  
Author(s):  
Alienke van Pijkeren ◽  
Jörn Dietze ◽  
Alejandro Sánchez Brotons ◽  
Tim Lijster ◽  
Andrei Barcaru ◽  
...  
Keyword(s):  
Histone Acetylation ◽  
Protein Modification ◽  
High Resolution Mass Spectrometry ◽  
Reaction Rates ◽  
Lysine Acetylation ◽  
Chemical Labeling ◽  
Comprehensive Description ◽  
Site Specific ◽  
New Approach

Histone acetylation is an important, reversible post-translational protein modification and a hallmark of epigenetic regulation. However, little is known about the dynamics of this process, due to the lack of analytical methods that can capture site-specific acetylation and deacetylation reactions. We present a new approach that combines metabolic and chemical labeling (CoMetChem) using uniformly 13C-labeled glucose and stable isotope labeled acetic anhydride. Thereby, chemically equivalent, fully acetylated histone species are generated enabling accurate relative quantification of site-specific lysine acetylation in tryptic peptides using high-resolution mass spectrometry. We show that CoMetChem enables site-specific quantification of the incorporation or loss of lysine acetylation over time, allowing the determination of reaction rates for acetylation and deacetylation. Thus, the CoMetChem methodology provides a comprehensive description of site-specific acetylation dynamics. <br>

Temporal- and Site-Specific Determination of the Origin of the Luminescent Bands in Silicon Nanowires

2008 ◽  
Vol 112 (36) ◽  
pp. 13943-13946 ◽  
Author(s):  
R. A. Rosenberg ◽  
G. K. Shenoy ◽  
P.-S. G. Kim ◽  
T. K. Sham
Keyword(s):  
Silicon Nanowires ◽  
Site Specific ◽  
Specific Determination

scholarly journals Combined Metabolic and Chemical (CoMetChem) Labeling Using Stable Isotopes – a Strategy to Reveal Site-Specific Histone Acetylation and Deacetylation Rates by LC-MS

2021 ◽  
Author(s):  
Alienke van Pijkeren ◽  
Jörn Dietze ◽  
Alejandro Sánchez Brotons ◽  
Tim Lijster ◽  
Andrei Barcaru ◽  
...  
Keyword(s):  
Histone Acetylation ◽  
Protein Modification ◽  
High Resolution Mass Spectrometry ◽  
Reaction Rates ◽  
Lysine Acetylation ◽  
Chemical Labeling ◽  
Comprehensive Description ◽  
Site Specific ◽  
New Approach

Histone acetylation is an important, reversible post-translational protein modification and a hallmark of epigenetic regulation. However, little is known about the dynamics of this process, due to the lack of analytical methods that can capture site-specific acetylation and deacetylation reactions. We present a new approach that combines metabolic and chemical labeling (CoMetChem) using uniformly 13C-labeled glucose and stable isotope labeled acetic anhydride. Thereby, chemically equivalent, fully acetylated histone species are generated enabling accurate relative quantification of site-specific lysine acetylation in tryptic peptides using high-resolution mass spectrometry. We show that CoMetChem enables site-specific quantification of the incorporation or loss of lysine acetylation over time, allowing the determination of reaction rates for acetylation and deacetylation. Thus, the CoMetChem methodology provides a comprehensive description of site-specific acetylation dynamics. <br>

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