Year: 2019
Type: review
Abstract: -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.
Source: mBio
Language: English
Subfield: Spectroscopy
Field: Chemistry
Domain: Physical Sciences
Open Access status: gold
Estimated APC paid: $3,900
Awards: G1689835210, G1788565809, Collaborative Research: RUI: Expanding the repertoire of chemical tools to study and characterize bacterial Gcn5-related N-acetyltransferase functions, Lysine Acetylation in N. gonorrhoeae Quorum Sensing and Biofilm Formation, G2657394853, TripleTOF 5600 High Resolution Mass Spectrometer, Sensing central metabolic stress
OpenAlex ID: W2938882297