Cutting to the quick: proteolytic control of oxygen sensors

Abstract

The several relationships amongst oxygen tension, oxygen-radical damage, and proteolysis have been the subject of intermittent studies since the 1940s.¹ Even in those early investigations, it was realised that gross oxidative damage to proteins could cause their unfolding and chemical modification, such that in cell-free systems either enhanced or reduced susceptibility to proteolytic enzymes results, depending on dose, protein and environment. More recent work has implied that these conclusions have some relevance to intact cells, though the precise mechanisms involved remain somewhat unclear (reviewed by Davies & Dean² and Dean et al.³).