scholarly journals The Leukemogenicity of AML1-ETO Is Dependent on Site-Specific Lysine Acetylation

Science ◽  
2011 ◽  
Vol 333 (6043) ◽  
pp. 765-769 ◽  
Author(s):  
L. Wang ◽  
A. Gural ◽  
X.-J. Sun ◽  
X. Zhao ◽  
F. Perna ◽  
...  
Keyword(s):  
Lysine Acetylation ◽  
Site Specific

The challenge of detecting modifications on proteins

2020 ◽  
Vol 64 (1) ◽  
pp. 135-153 ◽  
Author(s):  
Lauren Elizabeth Smith ◽  
Adelina Rogowska-Wrzesinska
Keyword(s):  
Mass Spectrometry ◽  
Protein Function ◽  
Chemical Properties ◽  
Lysine Acetylation ◽  
Mass Determination ◽  
Post Translational Modifications ◽  
Site Specific ◽  
The Common

Abstract Post-translational modifications (PTMs) are integral to the regulation of protein function, characterising their role in this process is vital to understanding how cells work in both healthy and diseased states. Mass spectrometry (MS) facilitates the mass determination and sequencing of peptides, and thereby also the detection of site-specific PTMs. However, numerous challenges in this field continue to persist. The diverse chemical properties, low abundance, labile nature and instability of many PTMs, in combination with the more practical issues of compatibility with MS and bioinformatics challenges, contribute to the arduous nature of their analysis. In this review, we present an overview of the established MS-based approaches for analysing PTMs and the common complications associated with their investigation, including examples of specific challenges focusing on phosphorylation, lysine acetylation and redox modifications.

scholarly journals Evaluating Mechanisms of IDH1 Regulation through Site-Specific Acetylation Mimics

Biomolecules ◽  
2021 ◽  
Vol 11 (5) ◽  
pp. 740
Author(s):  
Joi Weeks ◽  
Alexandra I. Strom ◽  
Vinnie Widjaja ◽  
Sati Alexander ◽  
Dahra K. Pucher ◽  
...  
Keyword(s):  
Isocitrate Dehydrogenase ◽  
Translational Regulation ◽  
Catalytic Efficiency ◽  
Low Grade ◽  
Lysine Acetylation ◽  
Site Specific ◽  
Idh1 Mutations ◽  
Mutant Idh1 ◽  
Biochemical Features ◽  
Secondary Glioblastomas

Isocitrate dehydrogenase (IDH1) catalyzes the reversible NADP+-dependent oxidation of isocitrate to α-ketoglutarate (αKG). IDH1 mutations, primarily R132H, drive > 80% of low-grade gliomas and secondary glioblastomas and facilitate the NADPH-dependent reduction of αKG to the oncometabolite D-2-hydroxyglutarate (D2HG). While the biochemical features of human WT and mutant IDH1 catalysis have been well-established, considerably less is known about mechanisms of regulation. Proteomics studies have identified lysine acetylation in WT IDH1, indicating post-translational regulation. Here, we generated lysine to glutamine acetylation mimic mutants in IDH1 to evaluate the effects on activity. We show that mimicking lysine acetylation decreased the catalytic efficiency of WT IDH1, with less severe catalytic consequences for R132H IDH1.

Site-Specific Identification of Lysine Acetylation Stoichiometries in Mammalian Cells

2016 ◽  
Vol 15 (3) ◽  
pp. 1103-1113 ◽  
Author(s):  
Tong Zhou ◽  
Ying-hua Chung ◽  
Jianji Chen ◽  
Yue Chen
Keyword(s):  
Mammalian Cells ◽  
Lysine Acetylation ◽  
Site Specific ◽  
Specific Identification

scholarly journals Site-Specific Reactivity of Nonenzymatic Lysine Acetylation

2015 ◽  
Vol 10 (1) ◽  
pp. 122-128 ◽  
Author(s):  
Josue Baeza ◽  
Michael J. Smallegan ◽  
John M. Denu
Keyword(s):  
Lysine Acetylation ◽  
Site Specific ◽  
Specific Reactivity

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>

scholarly journals Stoichiometry of Site-specific Lysine Acetylation in an Entire Proteome

2014 ◽  
Vol 289 (31) ◽  
pp. 21326-21338 ◽  
Author(s):  
Josue Baeza ◽  
James A. Dowell ◽  
Michael J. Smallegan ◽  
Jing Fan ◽  
Daniel Amador-Noguez ◽  
...  
Keyword(s):  
Lysine Acetylation ◽  
Site Specific
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