Poster abstracts

Poster number 26 submitted by Paula A Agudelo Garcia

Influence of HAT1 in Mitochondrial Function.

Paula A Agudelo Garcia (Molecular and Cellular Biochemistry, The Ohio State University)

Abstract:
Lysine acetylation is a reversible and highly regulated post-translational modification with a wide diversity of targets. Recently, this modification has emerged as an important potential regulatory mechanism in liver metabolism; different analyses have identified several mitochondrial proteins being acetylated in mouse liver providing a potential link between mitochondrial function and protein acetylation. Importantly, the substrate specificity of Lysine Acetyltransferases (KATs), with the exception of histones, is almost entirely uncharacterized. Our lab has developed a mouse knockout model for the first known protein lysine acetyltransferase HAT1 (also known as KAT1). Subcellular fractionation experiments have allowed us to detect the presence of this enzyme in mitochondrial extracts of mouse embryonic fibroblasts. Additionally knockout cells exhibit increased levels of reactive oxygen species and higher sensitivity to Antimycin A and nutrient deprivation, suggesting that HAT1 promotes mitochondrial function most likely through acetylation of metabolic proteins.

Keywords: HAT1, acetylation, mitochondria