Staufen2 is a neuronal RNA-binding protein that plays an important role in the differentiation of neural progenitor cells during neurogenesis. In addition, it is a key factor in the transport of RNA to synapses and is therefore important for synaptic plasticity, the basis of memory and memory formation.
The team led by Professor Dr. Dierk Niessing, group leader at the Institute of Structural Biology (STB) of Helmholtz Zentrum München and professor and head of the Institute of Pharmaceutical Biotechnology at the University of Ulm, showed that RNA-binding domains (dsRBDs) 1 and 2 of the mStau2 protein bond to mRNA with the same affinity and kinetics as domains 3 and 4. It was previously thought that the latter were in themselves sufficient for mRNA binding. While RNA recognition by each of these so-called tandem domains is transient, all four RNA-binding domains recognize their target RNA with a high degree of stability.
Studies - RNA - Domains - Staufen2 - Binding
Previous studies had suggested that only two RNA binding domains in Staufen2, namely dsRBD 3 and 4, are responsible for binding. Despite this, until now it proved impossible to reproduce stable binding required for RNA transport in the test tube. "That problem has been solved," says Niessing, "because it is now clear that dsRBDs 1 and 2 are also needed to create a stable complex. Using various biochemical and biophysical techniques, we were able to explain the behavior of dsRBD 1 and 2 ." "It...
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