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A team of scientists from Helmholtz Zentrum München and the University of Ulm has discovered that the neuronal transport factor Staufen2 scans and binds to its target transcripts in a much more complex manner than previously thought. RNA is transported within highly complex protein-RNA particles whose structure and specificity are still poorly understood. The team's findings, recently published in the journal Nature Communications, opens up new approaches to improve our understanding of the process.
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.
Team - Professor - Dr - Dierk - Niessing
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.
Previous studies had suggested that...
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