Niessing lab publishes structures of ASH1 mRNP in Nature Struct. Mol. Biol.

In this study the Niessing lab solved three X-ray structures to understand how the E3 localization element of the ASH1 mRNA is folded, how it is recognized in the nucleus by She2p, and how highly specific binding in the cytoplasmic is achieved by the additional joining of the myosin adapter She3p. Quite unexpectedly, the E3 element undergoes major rearrangements upon She2p binding. Furthermore, high RNA specificity in the cytoplasm is achieved through unstructured regions of She3p that introduce steric constraints. This work was performed in close collaboration with the Jansen lab of the FOR2333 team.

Edelmann FT, Schlundt A, Heym RG, Jenner A, Niedner-Boblenz A, Syed MI, Paillart J-C, Stehle R, Janowski R, Sattler M, Jansen R-P, Niessing D
Molecular architecture and dynamics of ASH1 mRNA recognition by its mRNA-transport complex
Nature Structural & Molecular Biology (2017) doi:10.1038/nsmb.3351