A5061584755- Heat shock proteins research
- Plant biochemistry and biosynthesis
- Toxin Mechanisms and Immunotoxins
- DNA Repair Mechanisms
- Plant Genetic and Mutation Studies
- Protein Structure and Dynamics
- Enzyme Structure and Function
University of North Carolina at Charlotte
2022-2024
The activity of the Hsp70 molecular chaperone is regulated by a suite helper co-chaperones that include J-proteins. Studies on J-proteins have historically focused their expression, localization, and activation Hsp70. There growing evidence post-translational modifications (PTMs) chaperones (the code) fine-tune function. This mini-review summarizes current understanding role regulation PTMs major Ydj1 DNAJA1. Understanding these may provide novel therapeutic avenues for targeting in cancer...
Proteostasis, the maintenance of cellular protein balance, is essential for cell viability and highly conserved across all organisms. Newly synthesized proteins, or “clients,” undergo sequential processing by Hsp40, Hsp70, Hsp90 chaperones to achieve proper folding functionality. Despite extensive characterization post-translational modifications (PTMs) on Hsp70 Hsp90, Hsp40 remain less understood. This study aims elucidate role lysine acetylation yeast Ydj1. By mutating sites Ydj1’s...
Molecular chaperones such as Hsp70 and Hsp90 help fold activate proteins in important signal transduction pathways that include DNA damage response (DDR). Previous studies have suggested the levels of mammalian APE2 exonuclease, a protein critical for repair, may be dependent on chaperone activity. In this study, we demonstrate budding yeast Apn2 exonuclease interacts with molecular Ssa1 Hsp82 co-chaperone Ydj1. Although does not display binding preference any specific cytosolic or paralog,...
Abstract Proteostasis, the maintenance of cellular protein balance, is essential for cell viability and highly conserved across all organisms. Newly synthesized proteins, or “clients,” undergo sequential processing by Hsp40, Hsp70, Hsp90 chaperones to achieve proper folding functionality. Despite extensive characterization post-translational modifications (PTMs) on Hsp70 Hsp90, Hsp40 remain less understood. This study aims elucidate role lysine acetylation yeast Ydj1. By mutating sites...