Abstract
Oxidative stress is a factor in a series of diseases and aging, primarily through irreversible oxidative modification of proteins. A major question is how nonenzymatic oxidation has the specificity to impact cellular regulation. Here, we report the degree to which in vivo protein oxidation to the ketone and aldehyde level is random using yeast as a simple model system and hydrogen peroxide as an environmental oxidative stress agent. Among 415 affinity-selected proteins identified throughout the matrix of stressed cells, oxidation sites were found in 87, predominantly on lysine, arginine, proline, histidine, threonine, and methionine residues. In almost all cases, one to two specific oxidation sites on the exterior of proteins were identified using MS-derived sequence and publicly available 3-D structural data. This suggests that, when regulation or disease progression is mediated by protein oxidation, specific new "allotypic active sites" are being created in proteins that trigger the process.
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