Mechanism of RNA stabilization and translational activation by a pentatricopeptide repeat protein
Open accessAbstract
Pentatricopeptide repeat (PPR) proteins comprise a large family of helical repeat proteins that bind RNA and modulate organellar RNA metabolism. The mechanisms underlying the functions attributed to PPR proteins are unknown. We describe in vitro studies of the maize protein PPR10 that clarify how PPR10 modulates the stability and translation of specific chloroplast mRNAs. We show that recombinant PPR10 bound to its native binding site in the chloroplast atpI-atpH intergenic region (i) blocks both 5'→3' and 3'→ 5 exoribonucleases in vitro; (ii) is sufficient to define the native processed atpH mRNA 5'-terminus in conjunction with a generic 5'→3' exoribonuclease; and (iii) remodels the structure of the atpH ribosome-binding site in a manner that can account for PPR10's ability to enhance atpH translation. In addition, we show that the minimal PPR10-binding site spans 17 nt. We propose that the site-specific barrier and RNA remodeling activities of PPR10 are a consequence of its unusually long, high-affinity interface with single-stranded RNA, that this interface provides a functional mimic to bacterial small RNAs, and that analogous activities underlie many of the biological functions that have been attributed to PPR proteins.
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The number of PPR motifs in C. albicans proteins identified by HMM algorithms might be underestimated because PPR proteins are expected to contain many motifs, each recognizing one nucleotide.
“As PPR proteins are expected to contain a multitude of PPR motifs, where each single motif recognizes one nucleotide in the RNA substrate (Prikryl et al. 2011), this number might be underestimated.”
From <i>Candida albicans</i> PPR proteins are required for the expression of respiratory Complex I subunits (2024) · cites this paper as Prikryl et al. 2011
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- Authors
- Prikryl, J., Rojas, M., Schuster, G., & Barkan, A.
- Affiliations
- University of Oregon (US)
- Technion – Israel Institute of Technology (IL)
- Corresponding author
- Barkan, Alice
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 2010-12-20
- Volume
- 108
- Issue
- 1
- Pages
- 415-420
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC3017144
- OpenAlex
- W2124987635
- Cited by
- 298
- References
- 48
- Citations by year
- 2026: 7 · 2025: 18 · 2024: 16 · 2023: 15 · 2022: 23 · 2021: 17 · 2020: 17 · 2019: 14 · 2018: 28 · 2017: 17 · 2016: 16 · 2015: 17 · 2014: 17 · 2013: 23 · 2012: 31
- FWCI
- 9.77
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Proceedings of the National Academy of Sciences (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Science Foundation (0940979)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Photosynthetic Processes and Mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA and protein synthesis mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA Research and Splicing
- Keywords
- pentatricopeptide repeat proteins, 5'-3' exoribonuclease, 3'-5' exoribonuclease, single-stranded RNA binding, maize
- MeSH terms
- Base Sequence, Binding Sites, Chloroplasts, Zea mays, Exoribonucleases, Molecular Sequence Data, Ribosomes, RNA Processing, Post-Transcriptional, RNA, Messenger, Protein Biosynthesis, Base Pairing, RNA Stability, Electrophoretic Mobility Shift Assay, Arabidopsis Proteins
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