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

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

Research output: Contribution to journalArticleResearchpeer-review

38 Citations (Scopus)

Abstract

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
Number of pages9
JournalNucleic Acids Research
Volume43
Issue number3
DOIs
Publication statusPublished - 1 Jan 2015
Externally publishedYes

Cite this