Biochemical characterizations of Pontocerebellar Hypoplasia linked mutations of Target of Egr1 (TOE1) reveal impacts on thermal stability, ribonuclease activity, and oligomerization
Biochemical characterizations reveal changes in thermal stability and ribonuclease activity due to TOE1 mutations linked to pontocerebellar hypoplasia.
Key Points
PCH7-linked mutations in TOE1 significantly reduce protein thermal stability, impacting its function.
Eight out of eleven TOE1 variants exhibit decreased thermal stability, while only two affect ribonuclease activity.
Utilizing AlphaFold predicted structures, the study examines enzymatic properties of TOE1 mutations in vitro.
The findings may inform potential therapeutic strategies and further studies on TOE1 function and regulation.