Abstract:
:The pentatricopeptide repeat (PPR) is a helical repeat motif found in an exceptionally large family of RNA-binding proteins that functions in mitochondrial and chloroplast gene expression. PPR proteins harbor between 2 and 30 repeats and typically bind single-stranded RNA in a sequence-specific fashion. However, the basis for sequence-specific RNA recognition by PPR tracts has been unknown. We used computational methods to infer a code for nucleotide recognition involving two amino acids in each repeat, and we validated this model by recoding a PPR protein to bind novel RNA sequences in vitro. Our results show that PPR tracts bind RNA via a modular recognition mechanism that differs from previously described RNA-protein recognition modes and that underpins a natural library of specific protein/RNA partners of unprecedented size and diversity. These findings provide a significant step toward the prediction of native binding sites of the enormous number of PPR proteins found in nature. Furthermore, the extraordinary evolutionary plasticity of the PPR family suggests that the PPR scaffold will be particularly amenable to redesign for new sequence specificities and functions.
journal_name
PLoS Genetjournal_title
PLoS geneticsauthors
Barkan A,Rojas M,Fujii S,Yap A,Chong YS,Bond CS,Small Idoi
10.1371/journal.pgen.1002910subject
Has Abstractpub_date
2012-01-01 00:00:00pages
e1002910issue
8eissn
1553-7390issn
1553-7404pii
PGENETICS-D-12-01004journal_volume
8pub_type
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