Sequence-specific binding of a chloroplast pentatricopeptide repeat protein to its native group II intron ligand.

ABSTRACT: Pentatricopeptide repeat (PPR) proteins are defined by degenerate 35-amino acid repeats that are related to the tetratricopeptide repeat (TPR). Most characterized PPR proteins mediate specific post-transcriptional steps in gene expression in mitochondria or chloroplasts. However, little is known about the structure of PPR proteins or the biochemical mechanisms through which they act. Here we establish features of PPR protein structure and nucleic acid binding activity through in vitro experiments with PPR5, which binds and stabilizes a chloroplast tRNA precursor harboring a group II intron. Recombinant PPR5 was shown to be monomeric by analytical ultracentrifugation and gel filtration. Circular dichroism spectroscopy showed that PPR5 has a high content of alpha helices, as predicted from t

SUBMITTER: Williams-Carrier R 

PROVIDER: S-EPMC2525963 | biostudies-literature | 2008 Sep

REPOSITORIES: biostudies-literature