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RNase II binds to RNase E and modulates its endoribonucleolytic activity in the cyanobacterium Anabaena PCC 7120
Zhou, Cong1; Zhang, Juyuan2; Hu, Xinyu1; Li, Changchang1; Wang, Li1; Huang, Qiaoyun1; Chen, Wenli1
2020-04-17
Source PublicationNUCLEIC ACIDS RESEARCH
ISSN0305-1048
Volume48Issue:7Pages:3922-3934
Abstract

In Escherichia co/i, 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 AIr1240, 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 AIr1240 is an exoribonuclease II (RNase II), as it only degrades nonstructured 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.

DOI10.1093/nar/gkaa092
Indexed BySCI
Language英语
WOS Research AreaBiochemistry & Molecular Biology
WOS SubjectBiochemistry & Molecular Biology
WOS IDWOS:000525957700040
WOS KeywordE CATALYTIC DOMAIN ; ESCHERICHIA-COLI ; RIBONUCLEASE-II ; POLYNUCLEOTIDE PHOSPHORYLASE ; PROTEIN INTERACTIONS ; MEMBRANE-BINDING ; CELL VIABILITY ; DEGRADATION ; DEGRADOSOME ; CLEAVAGE
PublisherOXFORD UNIV PRESS
Citation statistics
Cited Times:1[WOS]   [WOS Record]     [Related Records in WOS]
Document Type期刊论文
Identifierhttp://ir.ihb.ac.cn/handle/342005/36012
Collection藻类生物学及应用研究中心_期刊论文
Corresponding AuthorChen, Wenli
Affiliation1.Huazhong Agr Univ, State Key Lab Agr Microbiol, Wuhan 430070, Peoples R China
2.Chinese Acad Sci, Inst Hydrobiol, Key Lab Algal Biol, Wuhan 430070, Peoples R China
Recommended Citation
GB/T 7714
Zhou, Cong,Zhang, Juyuan,Hu, Xinyu,et al. RNase II binds to RNase E and modulates its endoribonucleolytic activity in the cyanobacterium Anabaena PCC 7120[J]. NUCLEIC ACIDS RESEARCH,2020,48(7):3922-3934.
APA Zhou, Cong.,Zhang, Juyuan.,Hu, Xinyu.,Li, Changchang.,Wang, Li.,...&Chen, Wenli.(2020).RNase II binds to RNase E and modulates its endoribonucleolytic activity in the cyanobacterium Anabaena PCC 7120.NUCLEIC ACIDS RESEARCH,48(7),3922-3934.
MLA Zhou, Cong,et al."RNase II binds to RNase E and modulates its endoribonucleolytic activity in the cyanobacterium Anabaena PCC 7120".NUCLEIC ACIDS RESEARCH 48.7(2020):3922-3934.
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