{"doi":"10.1261/rna.907608","title":"The RNase E/G-type endoribonuclease of higher plants is located in the chloroplast and cleaves RNA similarly to the <i>E. coli</i> enzyme","abstract":"<jats:p>RNase E is an endoribonuclease that has been studied primarily in <jats:italic>Escherichia coli</jats:italic>, where it is prominently involved in the processing and degradation of RNA. Homologs of bacterial RNase E are encoded in the nuclear genome of higher plants. RNA degradation in the chloroplast, an organelle that originated from a prokaryote similar to cyanobacteria, occurs via the polyadenylation-assisted degradation pathway. In <jats:italic>E. coli</jats:italic>, this process is probably initiated with the removal of 5′-end phosphates followed by endonucleolytic cleavage by RNase E. The plant homolog has been proposed to function in a similar way in the chloroplast. Here we show that RNase E of <jats:italic>Arabidopsis</jats:italic> is located in the soluble fraction of the chloroplast as a high molecular weight complex. In order to characterize its endonucleolytic activity, <jats:italic>Arabidopsis</jats:italic> RNase E was expressed in bacteria and analyzed. Similar to its <jats:italic>E. coli</jats:italic> counterpart, the endonucleolytic activity of the <jats:italic>Arabidopsis</jats:italic> enzyme depends on the number of phosphates at the 5′ end, is inhibited by structured RNA, and preferentially cleaves A/U-rich sequences. The enzyme forms an oligomeric complex of ∼680 kDa. The chloroplast localization and the similarity in the two enzymes' characteristics suggest that plant RNase E participates in the initial endonucleolytic cleavage of the polyadenylation-stimulated RNA degradation process in the chloroplast, perhaps in collaboration with the two other chloroplast endonucleases, RNase J and CSP41.</jats:p>","journal":"RNA","year":2008,"id":683472,"datarank":0.6435689161722588,"base_score":4.290459441148391,"endowment":4.290459441148391,"self_citation_contribution":0.6435689161722588,"citation_network_contribution":0.0,"self_endowment_contribution":0.6435689161722588,"citer_contribution":0.0,"corpus_percentile":null,"corpus_rank":null,"citation_count":72,"citer_count":0,"citers_with_citation_signal":0,"citers_with_endowment":0,"datacite_reuse_total":0,"is_dataset":false,"is_dataset_confidence":null,"is_data_producer":false,"deposit_databanks":null,"is_oa":false,"file_count":0,"downloads":0,"has_version_chain":false,"published_date":null,"fair_score":null,"fair_percentile":null,"algorithm_id":"datarank_citation_only_1hop_v6","ranking_scope":"data_only","authors":[{"id":1785446,"name":"Sharon Sheffy-Levin","orcid":null,"position":1,"is_corresponding":false},{"id":461997,"name":"Fabian Glaser","orcid":"0000-0003-4038-7185","position":2,"is_corresponding":false},{"id":1785448,"name":"Gadi Schuster","orcid":null,"position":3,"is_corresponding":false},{"id":1785444,"name":"Aleks Schein","orcid":null,"position":0,"is_corresponding":false}],"reference_count":0,"raw_metadata":{"has_enrichment":true,"resolved":true,"title":"The RNase E/G-type endoribonuclease of higher plants is located in the chloroplast and cleaves RNA similarly to the <i>E. coli</i> enzyme","abstract":"<jats:p>RNase E is an endoribonuclease that has been studied primarily in <jats:italic>Escherichia coli</jats:italic>, where it is prominently involved in the processing and degradation of RNA. Homologs of bacterial RNase E are encoded in the nuclear genome of higher plants. RNA degradation in the chloroplast, an organelle that originated from a prokaryote similar to cyanobacteria, occurs via the polyadenylation-assisted degradation pathway. In <jats:italic>E. coli</jats:italic>, this process is probably initiated with the removal of 5′-end phosphates followed by endonucleolytic cleavage by RNase E. The plant homolog has been proposed to function in a similar way in the chloroplast. Here we show that RNase E of <jats:italic>Arabidopsis</jats:italic> is located in the soluble fraction of the chloroplast as a high molecular weight complex. In order to characterize its endonucleolytic activity, <jats:italic>Arabidopsis</jats:italic> RNase E was expressed in bacteria and analyzed. Similar to its <jats:italic>E. coli</jats:italic> counterpart, the endonucleolytic activity of the <jats:italic>Arabidopsis</jats:italic> enzyme depends on the number of phosphates at the 5′ end, is inhibited by structured RNA, and preferentially cleaves A/U-rich sequences. The enzyme forms an oligomeric complex of ∼680 kDa. The chloroplast localization and the similarity in the two enzymes' characteristics suggest that plant RNase E participates in the initial endonucleolytic cleavage of the polyadenylation-stimulated RNA degradation process in the chloroplast, perhaps in collaboration with the two other chloroplast endonucleases, RNase J and CSP41.</jats:p>","is_dataset_classified":null,"base_score":4.290459441148391,"endowment":4.290459441148391,"datacite_reuse_total":0,"file_count":0,"downloads":0,"views":0,"has_version_chain":false,"is_dataset":false,"is_oa":false,"pmid":"18441049","pmcid":null,"openalex_id":"https://openalex.org/W2138935984","authors":[],"funders":[],"total_grants":0,"fwci":8.5361,"citation_percentile":0.97426547,"influential_citations":0,"citation_trend":[{"year":2012,"count":6},{"year":2013,"count":7},{"year":2014,"count":5},{"year":2015,"count":4},{"year":2016,"count":3},{"year":2017,"count":1},{"year":2018,"count":1},{"year":2019,"count":1},{"year":2020,"count":4},{"year":2021,"count":3},{"year":2022,"count":1},{"year":2023,"count":3},{"year":2024,"count":7},{"year":2025,"count":3},{"year":2026,"count":2}],"oa_status":"bronze","license":null,"oa_locations":[{"url":"http://rnajournal.cshlp.org/content/14/6/1057.full.pdf","host_type":"journal"},{"url":"http://rnajournal.cshlp.org/content/14/6/1057.full.pdf","host_type":"publisher"},{"url":"https://syndication.highwire.org/content/doi/10.1261/rna.907608","host_type":"publisher"},{"url":"https://doi.org/10.1261/rna.907608","host_type":"journal"},{"url":"https://pubmed.ncbi.nlm.nih.gov/18441049","host_type":"repository"},{"url":"https://www.ncbi.nlm.nih.gov/pmc/articles/2390796","host_type":"repository"},{"url":"http://rnajournal.cshlp.org/cgi/content/short/14/6/1057","host_type":"repository"}],"fields_of_study":["Legume Nitrogen Fixing Symbiosis","Photosynthetic Processes and Mechanisms","Plant Reproductive Biology","Amino Acid Sequence","Arabidopsis Proteins","Catalytic Domain","Chloroplasts","Endoribonucleases","Escherichia coli","Genes, Plant","Models, Molecular","Molecular Sequence Data","Molecular Weight","Oligoribonucleotides, Antisense","Photosynthesis","Polyadenylation","Protein Conformation","RNA Stability","RNA, Messenger"],"mesh_terms":["Amino Acid Sequence","Chloroplasts","Endoribonucleases","Escherichia coli","Models, Molecular","Molecular Sequence Data","Molecular Weight","Photosynthesis","Protein Conformation","RNA, Messenger","Genes, Plant","Catalytic Domain","Oligoribonucleotides, Antisense","RNA Stability","Polyadenylation","Arabidopsis Proteins"],"keywords":["Endoribonuclease","Biology","RNase P","Degradosome","RNA","Exoribonuclease","Arabidopsis","Exosome complex","RNase PH","Chloroplast","RNase MRP","Polyadenylation","Biochemistry","Ribonuclease III","Ribonuclease","Molecular biology","Mutant","Gene","RNA interference"],"sdg_mappings":[],"linked_datasets":[],"clinical_trials":[],"software_tools":[],"database_accessions":[],"source":"live","citation_network_status":"fetched"},"created_at":"2026-08-18T11:15:51.019637Z","pmid":null,"pmcid":null,"fwci":null,"citation_percentile":null,"influential_citations":0,"oa_status":null,"license":null,"views":0,"total_file_size_bytes":0,"version_count":0,"fair_f":null,"fair_a":null,"fair_i":null,"fair_r":null,"fair_zscore":null,"fair_rationale":null,"fair_model":null,"fair_agent_version":null,"fair_fulltext_source":null,"fair_has_llm":null,"fair_computed_at":null,"clinical_trials":[],"software_tools":[],"db_accessions":[],"linked_datasets":[],"topics":[]}