Georgia Institute of Technology College of Sciences

The stress condition calls for an adequate activity of key enzymatic systems of cellular defense. Massive protein destabilization and degradation is occurring in stressed cells. The rate of protein re-synthesis (DNA->RNA->protein) is inadequate to adapt to rapidly changing environment. Therefore, an alternative mechanism should exist maintaining sufficient activity of defense enzymes. Interestingly, more than 50% of enzymes consist of identical subunits which are forming multimeric interface. Stabilization of multimers is important for enzymatic activity. We found that it can be achieved by the formation of inter-subunit covalent bridges in response to stress conditions. It shows an elegance of the structure design that directs selective subunits linkage and increases enzyme's robustness and chances of cell survival during the stress. In contrast, modification of aminoacids involved in linkage leads to protein destabilization, unfolding and degradation. These results describe a new instantaneous mechanism of structural adaptation that controls enzymatic system under stress condition.