The design, characterisation and structure of a synthetic pentatricopeptide repeat protein. — ASN Events
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  2. Session 5: Poster Session A
  3. The design, characterisation and structure of a synthetic pentatricopeptide repeat protein.

The design, characterisation and structure of a synthetic pentatricopeptide repeat protein. (#183)

Benjamin S. Gully 1 , Kunal R. Shah 1 , Mihwa Lee 1 , Agata Sadowska 1 , Will A. Stanley 1 , Ian D. Small 2 , Charles S. Bond 1
  1. University of Western Australia, Crawley, WA, Australia
  2. ARC centre of excellence in Plant Energy Biology, University of Western Australia, Crawley, Western Australia, Australia

The super-family of pentatricopeptide repeat (PPR) proteins are characterised by tandem arrays of a degenerate 35-amino-acid motif1. PPR proteins are essential for organelle biogenesis, RNA editing and post-translational maturation in plants. With genetic mutations resulting in cytoplasmic male sterility, seed development and other phenotypic impairments. Recent developments in understanding the modular nature of sequence-specific RNA binding by PPR proteins2 have raised the possibility of de novo design of proteins with specific targets, for use in biotechnology. We here describe the design and production of a synthetic PPR protein based on the consensus sequence of the canonical PPR motifs with tailored RNA binding capabilities. We will present comprehensive data on the characterisation of one such protein, describing for the first time its crystal structure, expanding its importance as the first synthetic P-class PPR protein structure and comment on the potential for such synthetic PPR proteins in the future.

References

1 Small, I. D. & Peeters, N. The PPR motif - a TPR-related motif prevalent in plant organellar proteins. Trends Biochem Sci 25, 46-47 (2000).  

2 Barkan, A. et al. A combinatorial amino acid code for RNA recognition by pentatricopeptide repeat proteins. PLoS genetics 8, e1002910, doi:10.1371/journal.pgen.1002910 (2012).