An artificial PPR scaffold for programmable RNA recognition

Sandrine Coquille, Aleksandra Filipovska, Tiongsun Chia, Lional Rajappa, James P. Lingford, Muhammad F.M. Razif, Stéphane Thore () and Oliver Rackham ()
Additional contact information
Sandrine Coquille: University of Geneva
Aleksandra Filipovska: Harry Perkins Institute of Medical Research and Centre for Medical Research, The University of Western Australia
Tiongsun Chia: Harry Perkins Institute of Medical Research and Centre for Medical Research, The University of Western Australia
Lional Rajappa: University of Geneva
James P. Lingford: Harry Perkins Institute of Medical Research and Centre for Medical Research, The University of Western Australia
Muhammad F.M. Razif: Harry Perkins Institute of Medical Research and Centre for Medical Research, The University of Western Australia
Stéphane Thore: University of Geneva
Oliver Rackham: Harry Perkins Institute of Medical Research and Centre for Medical Research, The University of Western Australia

Nature Communications, 2014, vol. 5, issue 1, 1-9

Abstract: 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.

Date: 2014
References: Add references at CitEc
Citations:

Downloads: (external link)
https://www.nature.com/articles/ncomms6729 Abstract (text/html)

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:5:y:2014:i:1:d:10.1038_ncomms6729

Ordering information: This journal article can be ordered from
https://www.nature.com/ncomms/

DOI: 10.1038/ncomms6729

Access Statistics for this article

Nature Communications is currently edited by Nathalie Le Bot, Enda Bergin and Fiona Gillespie

More articles in Nature Communications from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().