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The NHL domain of BRAT is an RNA-binding domain that directly contacts the hunchback mRNA for regulation

Title data

Loedige, Inga ; Stotz, Mathias ; Qamar, Saadia ; Kramer, Katharina ; Hennig, Janosch ; Schubert, Thomas ; Löffler, Patrick ; Längst, Gernot ; Merkl, Rainer ; Urlaub, Henning ; Meister, Gunter:
The NHL domain of BRAT is an RNA-binding domain that directly contacts the hunchback mRNA for regulation.
In: Genes & Development. Vol. 28 (2014) Issue 7 . - pp. 749-764.
ISSN 1549-5477
DOI: https://doi.org/10.1101/gad.236513.113

Abstract in another language

The Drosophila protein brain tumor (Brat) forms a complex with Pumilio (Pum) and Nanos (Nos) to repress hunchback (hb) mRNA translation at the posterior pole during early embryonic development. It is currently thought that complex formation is initiated by Pum, which directly binds the hb mRNA and subsequently recruits Nos and Brat. Here we report that, in addition to Pum, Brat also directly interacts with the hb mRNA. We identify Brat-binding sites distinct from the Pum consensus motif and show that RNA binding and translational repression by Brat do not require Pum, suggesting so far unrecognized Pum-independent Brat functions. Using various biochemical and biophysical methods, we also demonstrate that the NHL (NCL-1, HT2A, and LIN-41) domain of Brat, a domain previously believed to mediate protein–protein interactions, is a novel, sequence-specific ssRNA-binding domain. The Brat-NHL domain folds into a six-bladed β propeller, and we identify its positively charged top surface as the RNA-binding site. Brat belongs to the functional diverse TRIM (tripartite motif)-NHL protein family. Using structural homology modeling, we predict that the NHL domains of all TRIM-NHL proteins have the potential to bind RNA, indicating that Brat is part of a conserved family of RNA-binding proteins.

Further data

Item Type: Article in a journal
Refereed: Yes
Keywords: BRAT; RNA binding; TRIM-NHL; gene regulation; hunchback; translational repression
Institutions of the University: 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: No
DDC Subjects: 500 Science > 540 Chemistry
500 Science > 570 Life sciences, biology
Date Deposited: 07 Oct 2021 13:38
Last Modified: 07 Oct 2021 13:38
URI: https://eref.uni-bayreuth.de/id/eprint/67246