ArticleThe Plant cell2003
Domain analysis of the chloroplast polynucleotide phosphorylase reveals discrete functions in RNA degradation, polyadenylation, and sequence homology with exosome proteins.
Article in The Plant cell, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed, 72 citations in OpenAlex.
- Human PNPase causes RNA stabilization and accumulation of R-loops in the Escherichia coli model system.Scientific reports · 2023Article
- Integrating physiology, genetics, and transcriptome to decipher a new thermo-sensitive and light-sensitive virescent leaf gene mutant in cucumber.Frontiers in plant science · 2022Article
- Organellar and Secretory Ribonucleases: Major Players in Plant RNA Homeostasis.Plant physiology · 2020Article
- Roles of Organellar RNA-Binding Proteins in Plant Growth, Development, and Abiotic Stress Responses.International journal of molecular sciences · 2020Review
- Systematic sequencing of chloroplast transcript termini from Arabidopsis thaliana reveals >200 transcription initiation sites and the extensive imprints of RNA-binding proteins and secondary structures.Nucleic acids research · 2019Article
- Functions of Conserved Domains of Human Polynucleotide Phosphorylase on RNA Oxidation.Insights of biomedical research · 2019Article
- Inhibition of homologous phosphorolytic ribonucleases by citrate may represent an evolutionarily conserved communicative link between RNA degradation and central metabolism.Nucleic acids research · 2017Article
- A novel RNA binding protein affects rbcL gene expression and is specific to bundle sheath chloroplasts in C4 plants.BMC plant biology · 2013Article
- The archaeal DnaG protein needs Csl4 for binding to the exosome and enhances its interaction with adenine-rich RNAs.RNA biology · 2013Article
- A mutation in PNPT1, encoding mitochondrial-RNA-import protein PNPase, causes hereditary hearing loss.American journal of human genetics · 2012Article
- Chloroplast RNase J compensates for inefficient transcription termination by removal of antisense RNA.RNA (New York, N.Y.) · 2011Article
- Review
- The exozyme model: a continuum of functionally distinct complexes.RNA (New York, N.Y.) · 2011Review
- Megadalton complexes in the chloroplast stroma of Arabidopsis thaliana characterized by size exclusion chromatography, mass spectrometry, and hierarchical clustering.Molecular & cellular proteomics : MCP · 2010Article
- Human mitochondrial SUV3 and polynucleotide phosphorylase form a 330-kDa heteropentamer to cooperatively degrade double-stranded RNA with a 3'-to-5' directionality.The Journal of biological chemistry · 2009Article
- Post-transcriptional control of chloroplast gene expression.Gene regulation and systems biology · 2009Article
- Crystal structure of Escherichia coli PNPase: central channel residues are involved in processive RNA degradation.RNA (New York, N.Y.) · 2008Article
- The RNase E/G-type endoribonuclease of higher plants is located in the chloroplast and cleaves RNA similarly to the E. coli enzyme.RNA (New York, N.Y.) · 2008Article
- Analysis of the human polynucleotide phosphorylase (PNPase) reveals differences in RNA binding and response to phosphate compared to its bacterial and chloroplast counterparts.RNA (New York, N.Y.) · 2008Article
- Integration of chloroplast nucleic acid metabolism into the phosphate deprivation response in Chlamydomonas reinhardtii.The Plant cell · 2007Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The molecular mechanism of mRNA degradation in the chloroplast consists of sequential events, including endonucleolytic cleavage, the addition of poly(A)-rich sequences to the endonucleolytic cleavage products, and exonucleolytic degradation. In spinach chloroplasts, the latter two steps of polyadenylation and exonucleolytic degradation are performed by the same phosphorolytic and processive enzyme, polynucleotide phosphorylase (PNPase). An analysis of its amino acid sequence shows that the protein is composed of two core domains related to RNase PH, two RNA binding domains (KH and S1), and an alpha-helical domain. The amino acid sequence and domain structure is largely conserved between bacteria and organelles. To define the molecular mechanism that controls the two opposite activities of this protein in the chloroplast, the ribonuclease, polymerase, and RNA binding properties of each domain were analyzed. The first core domain, which was predicted to be inactive in the bacterial enzymes, was active in RNA degradation but not in polymerization. Surprisingly, the second core domain was found to be active in degrading polyadenylated RNA only, suggesting that nonpolyadenylated molecules can be degraded only if tails are added, apparently by the same protein. The poly(A) high-binding-affinity site was localized to the S1 domain. The complete spinach chloroplast PNPase, as well as versions containing the core domains, complemented the cold sensitivity of an Escherichia coli PNPase-less mutant. Phylogenetic analyses of the two core domains showed that the two domains separated very early, resulting in the evolution of the bacterial and organelle PNPases and the exosome proteins found in eukaryotes and some archaea.
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