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Open Access Green möglich sobald Postprint bei der ZB eingereicht worden ist.
The NHL domain of BRAT is an RNA-binding domain that directly contacts the hunchback mRNA for regulation.
Genes Dev. 28, 749-764 (2014)
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 beta 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.
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Publikationstyp
Artikel: Journalartikel
Dokumenttyp
Wissenschaftlicher Artikel
Schlagwörter
Brat ; Rna Binding ; Trim-nhl ; Gene Regulation ; Hunchback ; Translational Repression; Drosophila Embryos; Stem-cells; Self-renewal; Microscale Thermophoresis; Beta-propeller; Protein; Pumilio; Tumor; Expression; Nanos
ISSN (print) / ISBN
0890-9369
e-ISSN
1549-5477
Zeitschrift
Genes and Development
Quellenangaben
Band: 28,
Heft: 7,
Seiten: 749-764
Verlag
Cold Spring Harbor Laboratory Press
Verlagsort
Cold Spring Harbor
Nichtpatentliteratur
Publikationen
Begutachtungsstatus
Peer reviewed
Institut(e)
Institute of Structural Biology (STB)