In vivo stabilization of endogenous chloroplast RNAs by customized artificial pentatricopeptide repeat proteins.

ABSTRACT: Pentatricopeptide repeat (PPR) proteins are helical repeat-proteins that bind RNA in a modular fashion with a sequence-specificity that can be manipulated by the use of an amino acid code. As such, PPR repeats are promising scaffolds for the design of RNA binding proteins for synthetic biology applications. However, the in vivo functional capabilities of artificial PPR proteins built from consensus PPR motifs are just starting to be explored. Here, we report in vivo functions of an artificial PPR protein, dPPRrbcL, made of consensus PPR motifs that were designed to bind a sequence near the 5' end of rbcL transcripts in Arabidopsis chloroplasts. We used a functional complementation assay to demonstrate that this protein bound its intended RNA target with specificity in vivo and that it subs

SUBMITTER: Manavski N 

PROVIDER: S-EPMC8191804 | biostudies-literature | 2021 Jun

REPOSITORIES: biostudies-literature