Molecular Characteristics of Lysine Deacetylase Interactions
Abstract
Lysine deacetylases (KDACs) mediate control of numerous cellular processes through the regulation of post-translational modification of lysine residues in substrate proteins. Our objective was to determine the molecular characteristics of the substrate binding surface of lysine deacetylases and the interactions of that surface with substrates and small molecule regulators. Key outcomes of our work include development of a novel, general-purpose assay for KDACs; determination that activator molecules of KDAC8 are not biologically relevant and only increase activity for enzyme preparations that are inherently low activity; characterization of the activity effects of fluorescent labels used in common KDAC assays; development of a reliable assay for T4 lysozyme; and development of robust expression, purification, and reaction conditions for KDACs. We also characterized the impact of several mutations to KDACs to gain insight into the biological roles of these enzymes.
Document Details
- Document Type
- Technical Report
- Publication Date
- Jun 15, 2017
- Accession Number
- AD1057223
Entities
People
- Terry J Watt
Organizations
- Xavier University of Louisiana