5KL1

Crystal structure of the Pumilio-Nos-hunchback RNA complex

5KL1 の概要

• エントリーDOI: 10.2210/pdb5kl1/pdb
• 関連するPDBエントリー: 5KL8 5KLA
• 分子名称: Maternal protein pumilio, Protein nanos, RNA (5'-R(*AP*AP*AP*UP*UP*GP*UP*AP*CP*AP*UP*A)-3'), ... (4 entities in total)
• 機能のキーワード: rna-binding proteins, rna binding protein-rna complex, rna binding protein/rna
• 由来する生物種: Drosophila melanogaster (Fruit fly); 詳細
• 細胞内の位置: Cytoplasm : P25822
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 56908.02

構造登録者

Qiu, C.,Hall, T.M.T. (登録日: 2016-06-23, 公開日: 2016-08-17, 最終更新日: 2023-09-27)

主引用文献

Weidmann, C.A.,Qiu, C.,Arvola, R.M.,Lou, T.F.,Killingsworth, J.,Campbell, Z.T.,Tanaka Hall, T.M.,Goldstrohm, A.C.
Drosophila Nanos acts as a molecular clamp that modulates the RNA-binding and repression activities of Pumilio.
Elife, 5:-, 2016

PubMed Abstract: Collaboration among the multitude of RNA-binding proteins (RBPs) is ubiquitous, yet our understanding of these key regulatory complexes has been limited to single RBPs. We investigated combinatorial translational regulation by Drosophila Pumilio (Pum) and Nanos (Nos), which control development, fertility, and neuronal functions. Our results show how the specificity of one RBP (Pum) is modulated by cooperative RNA recognition with a second RBP (Nos) to synergistically repress mRNAs. Crystal structures of Nos-Pum-RNA complexes reveal that Nos embraces Pum and RNA, contributes sequence-specific contacts, and increases Pum RNA-binding affinity. Nos shifts the recognition sequence and promotes repression complex formation on mRNAs that are not stably bound by Pum alone, explaining the preponderance of sub-optimal Pum sites regulated in vivo. Our results illuminate the molecular mechanism of a regulatory switch controlling crucial gene expression programs, and provide a framework for understanding how the partnering of RBPs evokes changes in binding specificity that underlie regulatory network dynamics.

PubMed: 27482653
DOI: 10.7554/eLife.17096

実験手法

X-RAY DIFFRACTION (3.701 Å)