Article
Allosteric modulation of the Lon protease via ssDNA binding and local charge changes.
The Journal of biological chemistry - 1 Jan 2025
Ogdahl Justyne L, Chien Peter
Abstract excerpt
The ATPase Associated with diverse cellular Activities (AAA+) family of proteases play crucial roles in cellular proteolysis and stress responses. Like other AAA + proteases, the Lon protease is known to be allosterically regulated by nucleotide and substrate binding. Although it was originally classified as a DNA binding protein, the impact of DNA binding on Lon activity is unclear. In this study, we...
Topics
- Protease La
- DNA, Single-Stranded
- Allosteric Regulation
- Adenosine Triphosphate
- Escherichia coli Proteins
- Protein Binding
- Mutation
- Escherichia coli