title: The solution structure of the pentatricopeptide repeat protein PPR10 upon binding atpH RNA.
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.
authors.affiliation: School of Chemistry and Biochemistry, The University of Western Australia, Crawley, Western Australia, Australia.
authors.forename: Benjamin S
authors.initials: BS
authors.lastname: Gully
authors.affiliation: SAXSWAXS beamline, Australian Synchrotron, 800 Blackburn Road, Clayton, Victoria, Australia.
authors.forename: Nathan
authors.initials: N
authors.lastname: Cowieson
authors.affiliation: School of Chemistry and Biochemistry, The University of Western Australia, Crawley, Western Australia, Australia Australian Research Council Centre of Excellence in Plant Energy Biology, The University of Western Australia, Crawley, Western Australia, Australia.
authors.forename: Will A
authors.initials: WA
authors.lastname: Stanley
authors.affiliation: School of Chemistry and Biochemistry, The University of Western Australia, Crawley, Western Australia, Australia Australian Research Council Centre of Excellence in Plant Energy Biology, The University of Western Australia, Crawley, Western Australia, Australia.
authors.forename: Kate
authors.initials: K
authors.lastname: Shearston
authors.affiliation: Australian Research Council Centre of Excellence in Plant Energy Biology, The University of Western Australia, Crawley, Western Australia, Australia.
authors.forename: Ian D
authors.initials: ID
authors.lastname: Small
authors.affiliation: Institute of Molecular Biology, University of Oregon, Eugene, Oregon, USA.
authors.forename: Alice
authors.initials: A
authors.lastname: Barkan
authors.affiliation: School of Chemistry and Biochemistry, The University of Western Australia, Crawley, Western Australia, Australia Charles.Bond@uwa.edu.au.
authors.forename: Charles S
authors.initials: CS
authors.lastname: Bond
mesh_terms: D002942:Circular Dichroism; D008958:Models, Molecular; D010940:Plant Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D018749:RNA, Plant / Q000378:metabolism*; D012542:Scattering, Radiation; D003313:Zea mays / Q000235:genetics / Q000378:metabolism*
chemical_list: D010940:Plant Proteins; D018749:RNA, Plant