Assembly of the ternary Brat-Pum-hb mRNA protein-RNA complex during embryonal development
RNAs and their interaction with RNA-binding proteins (RBPs) play a central role in the regulation of gene expression. Thus far the focus has mainly been on single RNA binding domains (RBDs) and the mechanism of interaction with their RNA target. However, specificity and affinity is often low for single RBDs to explain their biological function. Therefore, it is essential to explore how general but distinct RBPs bind together cooperatively to increase affinity and specificity to their cognate mRNA targets. Recently, we successfully combined X-ray crystallography, NMR and small-angle X-ray and neutron scattering to determine the structure of a ternary multi-protein RNA complex. In this new example here, we aim to determine the structure of another ternary complex consisting of two distinct RNA binding proteins. The NHL domain of Brat and the Pum-HD domain of Pumilio bind to hunchback mRNA to ensure proper embryonal development in flies. Both proteins have orthologs in humans and mutations in Brat orthologs TRIM2 and TRIM3 are linked developmental disorder in vertebrates. A detailed picture of the binding mechanism would extend our understanding of the protein-RNA recognition code.
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HENNIG Janosch; FOOT Jaelle; GABEL Frank and MARTEL Anne. (2016). Assembly of the ternary Brat-Pum-hb mRNA protein-RNA complex during embryonal development. Institut Laue-Langevin (ILL) doi:10.5291/ILL-DATA.8-03-870
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