<i>In vivo</i> 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 sequence-specificity can be manipulated by the use of an amino acid code. As such, PPR repeats promising scaffolds for design binding synthetic biology applications. However, vivo functional capabilities artificial built from consensus motifs just starting to explored. Here, we report functions protein, dPPRrbcL, made were designed sequence near 5? end rbcL transcripts Arabidopsis chloroplasts. We used complementation assay demonstrate this protein bound its intended target specificity and it substituted natural stabilizing processed mRNA. targeted second analogous petL UTR, where native PGR3, albeit inefficiently. These results showed engineered functionally mimic class serve as physical barriers against exoribonucleases.