Discipline: Chemistry and Chemical Sciences
Subcategory: Biochemistry (not Cell and Molecular Biology and Genetics)
Jatauria Lathan - Dillard University
Co-Author(s): Dr. Jiusheng Lin and Dr. Mark Wilson,University of Nebraska- Lincoln, Lincoln, Nebraska
HsDJ-1 is a 20 kDa neuroprotective, oxidative stress response protein that plays a key role in shielding cells against reactive oxygen species and mitochondrial damage. It contains an oxidation sensitive cysteine (C106), a highly conserved residue which is essential for DJ-1 to confer cellular protection. The oxidation of C106 is proposed to play an essential role in allowing DJ-1 to function as a redox sensor, although it may also provide a catalytic nucleophile for several proposed but unverified enzymatic activities of DJ-1. It has been recently reported that HsDJ-1 functions as a protein deglycase, removing the early glycation products formed when methylglyoxal (MG) reacts with proteins and nucleic acids. This hypothesis is important, as it would ascribe a long-sought enzymatic function to DJ1 and may help explain the protein’s involvement in several human disease states. HsDJ-1, HsDJ-1(O) HsDJ- 1 E18N, HsDJ-1 C106S, and HsDJ-1 E18D proteins were purified and utilized to test glycation activity. The glycation of N-acetyl- cysteine (NacCys) by methylglyoxal (MG) to form a hemithioacetal and its deglycation by DJ-1 was measured to quantify the enzymatic activity of DJ-1.Not Submitted
Funder Acknowledgement(s): This work was supported by NSF grant DBI-1461240 and the Nebraska Redox Biology Center REU program.
Faculty Advisor: Dr. Ruby Broadway, firstname.lastname@example.org
Role: My role in this research project was to purify the proteins that were used in the experiment as well as measure and record data obtained from enzymatic activity.