PuSH - Publication Server of Helmholtz Zentrum München: The crystal structure of the NHL domain in complex with RNA reveals the molecular basis of <em>Drosophila</em> brain-tumor-mediated gene regulation.

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Loedige, I.* ; Jakob, L.* ; Treiber, T.* ; Ray, D.W.* ; Stotz, M.* ; Treiber, N.* ; Hennig, J. ; Cook, K.B.* ; Morris, Q.* ; Hughes, T.R.* ; Engelmann, J.C.* ; Krahn, M.P.* ; Meister, G.*

The crystal structure of the NHL domain in complex with RNA reveals the molecular basis of Drosophila brain-tumor-mediated gene regulation.

Cell Rep. 13, 1206-1220 (2015)

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TRIM-NHL proteins are conserved among metazoans and control cell fate decisions in various stem cell linages. The Drosophila TRIM-NHL protein Brain tumor (Brat) directs differentiation of neuronal stem cells by suppressing self-renewal factors. Brat is an RNA-binding protein and functions as a translational repressor. However, it is unknown which RNAs Brat regulates and how RNA-binding specificity is achieved. Using RNA immunoprecipitation and RNAcompete, we identify Brat-bound mRNAs in Drosophila embryos and define consensus binding motifs for Brat as well as a number of additional TRIM-NHL proteins, indicating that TRIM-NHL proteins are conserved, sequence-specific RNA-binding proteins. We demonstrate that Brat-mediated repression and direct RNA-binding depend on the identified motif and show that binding of the localization factor Miranda to the Brat-NHL domain inhibits Brat activity. Finally, to unravel the sequence specificity of the NHL domain, we crystallize the Brat-NHL domain in complex with RNA and present a high-resolution protein-RNA structure of this fold.

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