Recent Progress Toward RNA Manipulation with Engineered Pentatricopeptide Repeat Proteins

Imai, Takayoshi; Yagi, Yusuke; Nakamura, Takahiro

doi:10.1007/978-981-10-8372-3_10

Cited by 1 publication

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References 44 publications

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“…From a biotechnological point of view, elucidating the PPR code is an opportunity area for the design of new RNA-binding proteins with a particular motif or additional domains bound to specific targets for the identification or control of mRNA metabolism. Imai et al (2018) suggest using PPR motifs as scaffolds to develop designed RNA-binding proteins. The fusion of PPR motifs with other domains could allow the development of new tools for (a) RNA detection in vivo by assembling engineered-PPR (ePPR) to a reporter protein (e.g., GFP); (b) translation regulation by fusing ePPR motif to eIF4G (eukaryotic translation initiation factor 4G), allowing activation translation of the targeted mRNA; (c) development of a site-specific endonuclease, by fusing ePPR motif with an endonuclease, which allows recognizing and cleaving RNA in a specific sequence; (d) RNA editing, using an ePPR protein with cytidine deaminase domains to catalyze cytosine's reaction to uracil at a specific position; and (e) finally, the use of engineered motifs targeted to otherwise naked or susceptible to degradation mRNA.…”

Section: Biotechnological Applications Of Ppr Tpr and Opr Proteinsmentioning

confidence: 99%

Pas de Trois: An Overview of Penta-, Tetra-, and Octo-Tricopeptide Repeat Proteins From Chlamydomonas reinhardtii and Their Role in Chloroplast Gene Expression

2021

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Penta-, Tetra-, and Octo-tricopeptide repeat (PPR, TPR, and OPR) proteins are nucleus-encoded proteins composed of tandem repeats of 35, 34, and 38–40 amino acids, respectively. They form helix-turn-helix structures that interact with mRNA or other proteins and participate in RNA stabilization, processing, maturation, and act as translation enhancers of chloroplast and mitochondrial mRNAs. These helical repeat proteins are unevenly present in plants and algae. While PPR proteins are more abundant in plants than in algae, OPR proteins are more abundant in algae. In Arabidopsis, maize, and rice there have been 450, 661, and 477 PPR proteins identified, respectively, which contrasts with only 14 PPR proteins identified in Chlamydomonas reinhardtii. Likewise, more than 120 OPR proteins members have been predicted from the nuclear genome of C. reinhardtii and only one has been identified in Arabidopsis thaliana. Due to their abundance in land plants, PPR proteins have been largely characterized making it possible to elucidate their RNA-binding code. This has even allowed researchers to generate engineered PPR proteins with defined affinity to a particular target, which has served as the basis to develop tools for gene expression in biotechnological applications. However, fine elucidation of the helical repeat proteins code in Chlamydomonas is a pending task. In this review, we summarize the current knowledge on the role PPR, TPR, and OPR proteins play in chloroplast gene expression in the green algae C. reinhardtii, pointing to relevant similarities and differences with their counterparts in plants. We also recapitulate on how these proteins have been engineered and shown to serve as mRNA regulatory factors for biotechnological applications in plants and how this could be used as a starting point for applications in algae.

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Section: Biotechnological Applications Of Ppr Tpr and Opr Proteinsmentioning

confidence: 99%

Pas de Trois: An Overview of Penta-, Tetra-, and Octo-Tricopeptide Repeat Proteins From Chlamydomonas reinhardtii and Their Role in Chloroplast Gene Expression

2021

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show abstract

Recent Progress Toward RNA Manipulation with Engineered Pentatricopeptide Repeat Proteins

Cited by 1 publication

References 44 publications

Pas de Trois: An Overview of Penta-, Tetra-, and Octo-Tricopeptide Repeat Proteins From Chlamydomonas reinhardtii and Their Role in Chloroplast Gene Expression

Pas de Trois: An Overview of Penta-, Tetra-, and Octo-Tricopeptide Repeat Proteins From Chlamydomonas reinhardtii and Their Role in Chloroplast Gene Expression

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