Structure of the Cmr2-Cmr3 subcomplex of the Cmr RNA silencing complex
| Autor: | Yaming Shao, Nancy F. Ramia, Michael P. Terns, Hong Li, Alexis I. Cocozaki, Rebecca M. Terns |
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| Rok vydání: | 2012 |
| Předmět: |
Protein subunit
Archaeal Proteins RNA-binding protein RNA Archaeal Biology Molecular Dynamics Simulation Crystallography X-Ray Protein Structure Secondary Article 03 medical and health sciences Structural Biology RNA interference Escherichia coli CRISPR Protein Interaction Domains and Motifs Molecular Biology 030304 developmental biology RNA Cleavage 0303 health sciences Binding Sites 030306 microbiology Protein Stability Ferredoxin fold RNA Molecular biology Recombinant Proteins Cell biology Pyrococcus furiosus RNA silencing Protein Subunits Mutation RNA Interference Protein Binding |
| Zdroj: | Structure (London, England : 1993). 21(3) |
| ISSN: | 1878-4186 |
| Popis: | SummaryThe Cmr complex is an RNA-guided effector complex that cleaves invader RNA in the prokaryotic immune response mediated by the CRISPR (Clustered Regularly Interspaced Short Palindromic Repeat)-Cas system. Here, we report the crystal structure of a Cmr subcomplex containing Cmr2 (Cas10) and Cmr3 subunits at 2.8 Å resolution. The structure revealed a dual ferredoxin fold and glycine-rich loops characteristic of previously known repeat-associated mysterious proteins and two unique insertion elements in Cmr3 that mediate its interaction with Cmr2. Surprisingly, while mutation of both insertion elements significantly weakened Cmr3-Cmr2 interaction, they exhibit differential effects on Cmr-mediated RNA cleavage by the Cmr complex, suggesting stabilization of Cmr2-Cmr3 interactions by other subunits. Further mutational analysis of the two conserved (but non-Cmr2-binding) glycine-rich loops of Cmr3 identified a region that is likely involved in assembly or the RNA cleavage function of the Cmr complex. |
| Databáze: | OpenAIRE |
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