5KL1

Crystal structure of the Pumilio-Nos-hunchback RNA complex

Summary for 5KL1

• Entry DOI: 10.2210/pdb5kl1/pdb
• Related: 5KL8 5KLA
• Descriptor: 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)
• Functional Keywords: rna-binding proteins, rna binding protein-rna complex, rna binding protein/rna
• Biological source: Drosophila melanogaster (Fruit fly); More
• Cellular location: Cytoplasm : P25822
• Total number of polymer chains: 3
• Total formula weight: 56908.02

Authors

Qiu, C.,Hall, T.M.T. (deposition date: 2016-06-23, release date: 2016-08-17, Last modification date: 2023-09-27)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (3.701 Å)