{"doi":"10.1093/nar/gkaa092","title":"RNase II binds to RNase E and modulates its endoribonucleolytic activity in the cyanobacterium Anabaena PCC 7120","abstract":"<jats:title>Abstract</jats:title><jats:p>In Escherichia coli, the endoribonuclease E (RNase E) can recruit several other ribonucleases and regulatory proteins via its noncatalytic domain to form an RNA degradosome that controls cellular RNA turnover. Similar RNA degradation complexes have been found in other bacteria; however, their compositions are varied among different bacterial species. In cyanobacteria, only the exoribonuclease PNPase was shown to bind to the noncatalytic domain of RNase E. Here, we showed that Alr1240, a member of the RNB family of exoribonucleases, could be co-isolated with RNase E from the lysate of the cyanobacterium Anabaena PCC 7120. Enzymatic analysis revealed that Alr1240 is an exoribonuclease II (RNase II), as it only degrades non-structured single-stranded RNA substrates. In contrast to known RNase E-interacting ribonucleases, which bind to the noncatalytic domain of RNase E, the Anabaena RNase II was shown to associate with the catalytic domain of RNase E. Using a strain in which RNase E and RNase II were tagged in situ with GFP and BFP, respectively, we showed that RNase E and RNase II form a compact complex in vivo by a fluorescence resonance energy transfer (FRET) assay. RNase E activity on several synthetic substrates was boosted in the presence of RNase II, suggesting that the activity of RNase E could be regulated by RNase II-RNase E interaction. To our knowledge, Anabaena RNase II is an unusual ribonuclease that interacts with the catalytic domain of RNase E, and it may represent a new type of RNA degradosome and a novel mechanism for regulating the activity of the RNA degradosome. As Anabaena RNase E interacts with RNase II and PNPase via different regions, it is very likely that the three ribonucleases form a large complex and cooperatively regulate RNA metabolism in the cell.</jats:p>","journal":"Nucleic Acids Research","year":2020,"id":658012,"datarank":0.70613104567643,"base_score":3.2188758248682006,"endowment":3.2188758248682006,"self_citation_contribution":0.48283137373023016,"citation_network_contribution":0.2232996719461999,"self_endowment_contribution":0.48283137373023016,"citer_contribution":0.2232996719461999,"corpus_percentile":null,"corpus_rank":null,"citation_count":24,"citer_count":14,"citers_with_citation_signal":9,"citers_with_endowment":9,"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":1717696,"name":"Juyuan Zhang","orcid":null,"position":1,"is_corresponding":false},{"id":1459520,"name":"Xinyu Hu","orcid":"0000-0002-9211-1765","position":2,"is_corresponding":false},{"id":1421250,"name":"Changchang Li","orcid":"0000-0001-5066-6968","position":3,"is_corresponding":false},{"id":346834,"name":"Li Wang","orcid":"0000-0003-4959-0729","position":4,"is_corresponding":false},{"id":1717697,"name":"Qiaoyun Huang","orcid":null,"position":5,"is_corresponding":false},{"id":510214,"name":"Wenli Chen","orcid":"0000-0002-6486-0582","position":6,"is_corresponding":false},{"id":434256,"name":"Cong Zhou","orcid":"0000-0002-6938-4685","position":0,"is_corresponding":false}],"reference_count":0,"raw_metadata":{"has_enrichment":true,"resolved":true,"title":"RNase II binds to RNase E and modulates its endoribonucleolytic activity in the cyanobacterium Anabaena PCC 7120","abstract":"<jats:title>Abstract</jats:title><jats:p>In Escherichia coli, the endoribonuclease E (RNase E) can recruit several other ribonucleases and regulatory proteins via its noncatalytic domain to form an RNA degradosome that controls cellular RNA turnover. Similar RNA degradation complexes have been found in other bacteria; however, their compositions are varied among different bacterial species. In cyanobacteria, only the exoribonuclease PNPase was shown to bind to the noncatalytic domain of RNase E. Here, we showed that Alr1240, a member of the RNB family of exoribonucleases, could be co-isolated with RNase E from the lysate of the cyanobacterium Anabaena PCC 7120. Enzymatic analysis revealed that Alr1240 is an exoribonuclease II (RNase II), as it only degrades non-structured single-stranded RNA substrates. In contrast to known RNase E-interacting ribonucleases, which bind to the noncatalytic domain of RNase E, the Anabaena RNase II was shown to associate with the catalytic domain of RNase E. Using a strain in which RNase E and RNase II were tagged in situ with GFP and BFP, respectively, we showed that RNase E and RNase II form a compact complex in vivo by a fluorescence resonance energy transfer (FRET) assay. RNase E activity on several synthetic substrates was boosted in the presence of RNase II, suggesting that the activity of RNase E could be regulated by RNase II-RNase E interaction. To our knowledge, Anabaena RNase II is an unusual ribonuclease that interacts with the catalytic domain of RNase E, and it may represent a new type of RNA degradosome and a novel mechanism for regulating the activity of the RNA degradosome. As Anabaena RNase E interacts with RNase II and PNPase via different regions, it is very likely that the three ribonucleases form a large complex and cooperatively regulate RNA metabolism in the cell.</jats:p>","is_dataset_classified":null,"base_score":3.2188758248682006,"endowment":3.2188758248682006,"datacite_reuse_total":0,"file_count":0,"downloads":0,"views":0,"has_version_chain":false,"is_dataset":false,"is_oa":false,"pmid":"32055835","pmcid":"PMC7144899","openalex_id":"https://openalex.org/W3006396851","authors":[],"funders":[{"funder_name":"National Natural Science Foundation of China","grant_id":"31570048","title":null},{"funder_name":"National Key Research and Development Program of China","grant_id":"2018YFE0105600","title":null},{"funder_name":"Chinese Academy of Sciences","grant_id":"Y65Z021501","title":null}],"total_grants":3,"fwci":0.6718,"citation_percentile":0.65052004,"influential_citations":0,"citation_trend":[{"year":2019,"count":1},{"year":2020,"count":1},{"year":2021,"count":2},{"year":2022,"count":2},{"year":2023,"count":4},{"year":2024,"count":6},{"year":2025,"count":8}],"oa_status":"gold","license":"cc-by-nc","oa_locations":[{"url":"https://academic.oup.com/nar/article-pdf/48/7/3922/33030761/gkaa092.pdf","host_type":"journal"},{"url":"https://academic.oup.com/nar/article-pdf/48/7/3922/33030761/gkaa092.pdf","host_type":"publisher"},{"url":"http://academic.oup.com/nar/article-pdf/48/7/3922/33030761/gkaa092.pdf","host_type":"publisher"},{"url":"https://doi.org/10.1093/nar/gkaa092","host_type":"journal"},{"url":"https://pubmed.ncbi.nlm.nih.gov/32055835","host_type":"repository"},{"url":"https://www.ncbi.nlm.nih.gov/pmc/articles/7144899","host_type":"repository"},{"url":"http://ir.ihb.ac.cn/handle/342005/36010","host_type":""},{"url":"http://ir.ihb.ac.cn/handle/342005/36011","host_type":""},{"url":"https://europepmc.org/articles/PMC7144899","host_type":"Europe_PMC"},{"url":"https://europepmc.org/articles/PMC7144899?pdf=render","host_type":"Europe_PMC"}],"fields_of_study":["Photosynthetic Processes and Mechanisms","Bacterial Genetics and Biotechnology","Microbial Metabolic Engineering and Bioproduction","Anabaena","Binding Sites","Catalytic Domain","Cytoplasm","Endoribonucleases","Exoribonucleases"],"mesh_terms":["Binding Sites","Cytoplasm","Endoribonucleases","Exoribonucleases","Anabaena","Catalytic Domain"],"keywords":["Biology","RNase P","Anabaena","Cyanobacteria","Biochemistry","RNase H","Microbiology","Genetics","RNA","Bacteria","Gene"],"sdg_mappings":[{"sdg_number":0,"sdg_label":"Affordable and clean energy"}],"linked_datasets":[],"clinical_trials":[],"software_tools":[],"database_accessions":[{"name":"gen"},{"name":"pdb"},{"name":"doi"}],"source":"live","citation_network_status":"fetched"},"created_at":"2026-08-12T03:01:04.603909Z","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":[]}