Abstract：
:Pentatricopeptide repeat (PPR) proteins control diverse aspects of RNA metabolism in eukaryotic cells. Although recent computational and structural studies have provided insights into RNA recognition by PPR proteins, their highly insoluble nature and inconsistencies between predicted and observed modes of RNA binding have restricted our understanding of their biological functions and their use as tools. Here we use a consensus design strategy to create artificial PPR domains that are structurally robust and can be programmed for sequence-specific RNA binding. The atomic structures of these artificial PPR domains elucidate the structural basis for their stability and modelling of RNA-protein interactions provides mechanistic insights into the importance of RNA-binding residues and suggests modes of PPR-RNA association. The modular mode of RNA binding by PPR proteins holds great promise for the engineering of new tools to target RNA and to understand the mechanisms of gene regulation by natural PPR proteins.
journal_name
Nat Communjournal_title
Nature communicationsauthors
Coquille S,Filipovska A,Chia T,Rajappa L,Lingford JP,Razif MF,Thore S,Rackham Odoi
10.1038/ncomms6729subject
Has Abstractpub_date
2014-12-17 00:00:00pages
5729issn
2041-1723pii
ncomms6729journal_volume
5pub_type
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