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

Loedige, I., Stotz, M., Qamar, S., Kramer, K., Hennig, J., Schubert, T., et al. (2014). The NHL domain of BRAT is an RNA-binding domain that directly contacts the hunchback mRNA for regulation. Genes and Development, 28(7), 749-764. doi:10.1101/gad.236513.113.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0019-1843-D Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0029-C048-8
Genre: Journal Article

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 Creators:
Loedige, I., Author
Stotz, M., Author
Qamar, S.1, Author              
Kramer, K.1, Author              
Hennig, J., Author
Schubert, T., Author
Löffler, P., Author
Längst, G., Author
Merkl, R., Author
Urlaub, H.1, Author              
Meister, G., Author
Affiliations:
1Research Group of Bioanalytical Mass Spectrometry, MPI for biophysical chemistry, Max Planck Society, ou_578613              

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Free keywords: BRAT; RNA binding; TRIM-NHL; gene regulation; hunchback; translational repression
 Abstract: 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.

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Language(s): eng - English
 Dates: 2014-04-01
 Publication Status: Published in print
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 Rev. Method: Peer
 Identifiers: DOI: 10.1101/gad.236513.113
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Title: Genes and Development
Source Genre: Journal
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Pages: - Volume / Issue: 28 (7) Sequence Number: - Start / End Page: 749 - 764 Identifier: -