6nww
From Proteopedia
Crystal structure of the RRM domain of S. pombe Puf1 in the P212121 space group
Structural highlights
FunctionPublication Abstract from PubMedPUF proteins, named for Drosophila Pumilio (PUM) and Caenorhabditis elegans fem-3-binding factor (FBF), recognize specific sequences in the mRNAs they bind and control. RNA binding by classical PUF proteins is mediated by a characteristic PUM homology domain (PUM-HD). The Puf1 and Puf2 proteins possess a distinct architecture and comprise a highly conserved subfamily among fungal species. Puf1/Puf2 proteins contain two types of RNA-binding domain: a divergent PUM-HD and an RNA recognition motif (RRM). They recognize RNAs containing UAAU motifs, often in clusters. Here, we report a crystal structure of the PUM-HD of a fungal Puf1 in complex with a dual UAAU motif RNA. Each of the two UAAU tetranucleotides are bound by a Puf1 PUM-HD forming a 2:1 protein-to-RNA complex. We also determined crystal structures of the Puf1 RRM domain that identified a dimerization interface. The PUM-HD and RRM domains act in concert to determine RNA-binding specificity: the PUM-HD dictates binding to UAAU, and dimerization of the RRM domain favors binding to dual UAAU motifs rather than a single UAAU. Cooperative action of the RRM and PUM-HD identifies a new mechanism by which multiple RNA-binding modules in a single protein collaborate to create a unique RNA-binding specificity. Distinct RNA-binding modules in a single PUF protein cooperate to determine RNA specificity.,Qiu C, Dutcher RC, Porter DF, Arava Y, Wickens M, Hall TMT Nucleic Acids Res. 2019 Sep 19;47(16):8770-8784. doi: 10.1093/nar/gkz583. PMID:31294800[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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