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Structure and dynamics of the quaternary hunchback mRNA translation repression complex

Title data

Macošek, Jakub ; Simon, Bernd ; Linse, Johanna-Barbara ; Jagtap, Pravin Kumar Ankush ; Winter, Sophie L. ; Foot, Jaelle ; Lapouge, Karine ; Perez, Kathryn ; Rettel, Mandy ; Ivanović, Miloš T. ; Masiewicz, Pawel ; Murciano, Brice ; Savitski, Mikhail M. ; Loedige, Inga ; Hub, Jochen S. ; Gabel, Frank ; Hennig, Janosch:
Structure and dynamics of the quaternary hunchback mRNA translation repression complex.
In: Nucleic Acids Research. Vol. 49 (2021) Issue 15 . - pp. 8866-8885.
ISSN 1362-4962
DOI: https://doi.org/10.1093/nar/gkab635

Project information

Project financing: Deutsche Forschungsgemeinschaft

Abstract in another language

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.

Further data

Item Type: Article in a journal
Refereed: Yes
Institutions of the University: Faculties
Faculties > Faculty of Biology, Chemistry and Earth Sciences
Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry
Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry > Chair Biochemistry with an Emphasis on Biophysical Chemistry
Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry > Chair Biochemistry with an Emphasis on Biophysical Chemistry > Chair Biochemistry with an Emphasis on Biophysical Chemistry - Univ.-Prof. Dr. Janosch Hennig
Result of work at the UBT: Yes
DDC Subjects: 500 Science > 540 Chemistry
500 Science > 570 Life sciences, biology
Date Deposited: 09 Sep 2021 07:49
Last Modified: 06 Oct 2021 06:58
URI: https://eref.uni-bayreuth.de/id/eprint/66989