The solution structure of the pentatricopeptide repeat protein PPR10 upon binding atpH RNA

Benjamin Gully, Nathan Cowieson, William Stanley, Kate Shearston, Ian Small, Alice Barkan, Charles S. Bond

Research output: Contribution to journalArticlepeer-review

46 Citations (Scopus)


© The Author(s) 2015. Published by Oxford University Press on behalf of Nucleic Acids Research. The pentatricopeptide repeat (PPR) protein family is a large family of RNA-binding proteins that is characterized by tandem arrays of a degenerate 35-amino-acid motif which form an α-solenoid structure. PPR proteins influence the editing, splicing, translation and stability of specific RNAs in mitochondria and chloroplasts. Zea mays PPR10 is amongst the best studied PPR proteins, where sequence-specific binding to two RNA transcripts, atpH and psaJ, has been demonstrated to follow a recognition code where the identity of two amino acids per repeat determines the base-specificity. A recently solved ZmPPR10:psaJ complex crystal structure suggested a homodimeric complex with considerably fewer sequence-specific protein - RNA contacts than inferred previously. Here we describe the solution structure of the ZmPPR10:atpH complex using size-exclusion chromatography-coupled synchrotron small-angle X-ray scattering (SEC-SY-SAXS). Our results support prior evidence that PPR10 binds RNA as a monomer, and that it does so in a manner that is commensurate with a canonical and predictable RNA-binding mode across much of the RNA - protein interface.
Original languageEnglish
Pages (from-to)1918-1926
JournalNucleic Acids Research
Issue number3
Early online date21 Jan 2015
Publication statusPublished - 18 Feb 2015


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