Relaxed Cleavage Specificity of Hyperactive Variants of Escherichia coli RNase E on RNA Iopen access
- Authors
- Bae, Dayeong; Hyeon, Hana; Shin, Eunkyoung; Yeom, Ji-Hyun; Lee, Kangseok
- Issue Date
- Feb-2023
- Publisher
- The Korean Society for Mocrobiology / The Korean Society of Virology
- Keywords
- Cleavage specificity; Endoribonuclease; Plasmid copy number; RNA I; RNase E
- Citation
- Journal of Microbiology, v.61, no.2, pp 211 - 220
- Pages
- 10
- Journal Title
- Journal of Microbiology
- Volume
- 61
- Number
- 2
- Start Page
- 211
- End Page
- 220
- URI
- https://scholarworks.bwise.kr/cau/handle/2019.sw.cau/66372
- DOI
- 10.1007/s12275-023-00013-z
- ISSN
- 1225-8873
1976-3794
- Abstract
- RNase E is an essential enzyme in Escherichia coli. The cleavage site of this single-stranded specific endoribonuclease is well-characterized in many RNA substrates. Here, we report that the upregulation of RNase E cleavage activity by a mutation that affects either RNA binding (Q36R) or enzyme multimerization (E429G) was accompanied by relaxed cleavage specificity. Both mutations led to enhanced RNase E cleavage in RNA I, an antisense RNA of ColE1-type plasmid replication, at a major site and other cryptic sites. Expression of a truncated RNA I with a major RNase E cleavage site deletion at the 5′-end (RNA I-5) resulted in an approximately twofold increase in the steady-state levels of RNA I-5 and the copy number of ColE1-type plasmid in E. coli cells expressing wild-type or variant RNase E compared to those expressing RNA I. These results indicate that RNA I-5 does not efficiently function as an antisense RNA despite having a triphosphate group at the 5′-end, which protects the RNA from ribonuclease attack. Our study suggests that increased cleavage rates of RNase E lead to relaxed cleavage specificity on RNA I and the inability of the cleavage product of RNA I as an antisense regulator in vivo does not stem from its instability by having 5′-monophosphorylated end. © 2023, The Author(s), under exclusive licence to Microbiological Society of Korea.
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