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Article Dans Une Revue Nucleic Acids Research Année : 2021

Structure and dynamics of the quaternary hunchback mRNA translation repression complex

Résumé

A key regulatory process during $Drosophila$ development is the localized suppression of the $hunchback$ mRNA translation at the posterior, which gives rise to a hunchback gradient governing the formation of the anterior-posterior body axis. This suppression is achieved by a concerted action of Brain Tumour (Brat), Pumilio (Pum) and Nanos. Each protein is necessary for proper $Drosophila$ development. The RNA contacts have been elucidated for the proteins individually in several atomic-resolution structures. However, the interplay of all three proteins during RNA suppression remains a long-standing open question. Here, we characterize the quaternary complex of the RNA-binding domains of Brat, Pum and Nanos with $hunchback$ mRNA by combining NMR spectroscopy, SANS/SAXS, XL/MS with MD simulations and ITC assays. The quaternary $hunchback$ mRNA suppression complex comprising the RNA binding domains is flexible with unoccupied nucleotides functioning as a flexible linker between the Brat and Pum-Nanos moieties of the complex. Moreover, the presence of the Pum-HD/Nanos-ZnF complex has no effect on the equilibrium RNA binding affinity of the Brat RNA binding domain. This is in accordance with previous studies, which showed that Brat can suppress mRNA independently and is distributed uniformly throughout the embryo.
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hal-03335234 , version 1 (06-09-2021)

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Jakub Macošek, Bernd Simon, Johanna-Barbara Linse, Pravin Kumar Ankush Jagtap, Sophie L. Winter, et al.. Structure and dynamics of the quaternary hunchback mRNA translation repression complex. Nucleic Acids Research, 2021, 49 (15), pp.8866-8885. ⟨10.1093/nar/gkab635⟩. ⟨hal-03335234⟩
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