Structures of Human Pumilio with Noncognate RNAs Reveal Molecular Mechanisms for Binding Promiscuity
| Autor: | Robin P. Wharton, Deepak T. Nair, Aneel K. Aggarwal, Yogesh K. Gupta |
|---|---|
| Rok vydání: | 2008 |
| Předmět: |
Models
Molecular Cyclin B Biology Crystallography X-Ray Structural Biology Humans Nucleotide Amino Acid Sequence RNA Messenger Binding site Molecular Biology chemistry.chemical_classification Binding Sites Base Sequence RNA-Binding Proteins RNA Molecular biology Protein Structure Tertiary Cell biology Promiscuity chemistry Regulatory sequence Sequence Alignment Protein Binding Transcription Factors |
| Zdroj: | Structure. 16:549-557 |
| ISSN: | 0969-2126 |
| Popis: | Summary Pumilio is a founder member of the evolutionarily conserved Puf family of RNA-binding proteins that control a number of physiological processes in eukaryotes. A structure of human Pumilio (hPum) Puf domain bound to a Drosophila regulatory sequence showed that each Puf repeat recognizes a single nucleotide. Puf domains in general bind promiscuously to a large set of degenerate sequences, but the structural basis for this promiscuity has been unclear. Here, we describe the structures of hPum Puf domain complexed to two noncognate RNAs, CycB reverse and Puf5. In each complex, one of the nucleotides is ejected from the binding surface, in effect, acting as a "spacer." The complexes also reveal the plasticity of several Puf repeats, which recognize noncanonical nucleotides. Together, these complexes provide a molecular basis for recognition of degenerate binding sites, which significantly increases the number of mRNAs targeted for regulation by Puf proteins in vivo. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|