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Structural basis for RNA recognition by a dimeric PPR-protein complex.
- Source :
-
Nature structural & molecular biology [Nat Struct Mol Biol] 2013 Dec; Vol. 20 (12), pp. 1377-82. Date of Electronic Publication: 2013 Nov 03. - Publication Year :
- 2013
-
Abstract
- Thylakoid assembly 8 (THA8) is a pentatricopeptide repeat (PPR) RNA-binding protein required for the splicing of the transcript of ycf3, a gene involved in chloroplast thylakoid-membrane biogenesis. Here we report the identification of multiple THA8-binding sites in the ycf3 intron and present crystal structures of Brachypodium distachyon THA8 either free of RNA or bound to two of the identified RNA sites. The apostructure reveals a THA8 monomer with five tandem PPR repeats arranged in a planar fold. The complexes of THA8 bound to the two short RNA fragments surprisingly reveal asymmetric THA8 dimers with the bound RNAs at the dimeric interface. RNA binding induces THA8 dimerization, with a conserved G nucleotide of the bound RNAs making extensive contacts with both monomers. Together, these results establish a new model of RNA recognition by RNA-induced formation of an asymmetric dimer of a PPR protein.
- Subjects :
- Binding Sites
Brachypodium metabolism
Crystallography, X-Ray
Dimerization
Introns
Models, Genetic
Models, Molecular
Plant Proteins genetics
Plant Proteins metabolism
Protein Structure, Tertiary
RNA, Plant chemistry
RNA-Binding Proteins genetics
RNA-Binding Proteins metabolism
Thylakoids metabolism
Brachypodium genetics
Plant Proteins chemistry
RNA, Plant metabolism
RNA-Binding Proteins chemistry
Subjects
Details
- Language :
- English
- ISSN :
- 1545-9985
- Volume :
- 20
- Issue :
- 12
- Database :
- MEDLINE
- Journal :
- Nature structural & molecular biology
- Publication Type :
- Academic Journal
- Accession number :
- 24186060
- Full Text :
- https://doi.org/10.1038/nsmb.2710