In this publication, Kim Lühmann and colleagues from the Kehr group used microscale thermophoresis to assess the RNA binding properties of glycine-rich RNA binding protein 7 (GRP7). The biological functions of GRP7 e.g. in alternative splicing and cold stress response depend on RNA binding. These results show that GRP7 has high affinity for a variety of RNAs and no or only a low selectivity for certain types of RNAs. The arginine-glycine-glycine (RGG) -domain plays a crucial role in binding longer RNAs and phase separation.
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Figure 2a: Comparison of dissociation constants (Kds) of AtGRP7 for RNAs varying in length, with and without UTRs and Introns, as well as single and double stranded RNA. (a) Kds of AtGRP7 for RNAs varying in length displayed in a bar graph. The length of RNAs is shown on the X-axis, the Y-axis shows the Kd in μM. Kds were compared by one-way ANOVA and Tukeys test (p = 0.01). Similar letters indicate no significant difference.
