Studies on a Vibrio vulnificus Functional Ortholog of Escherichia coli RNase E Imply a Conserved Function of RNase E-like Enzymes in Bacteria
- Authors
- Lee ,Minho; Yeom ,Ji-Hyun; Jeon, Che Ok; Lee, Kangseok
- Issue Date
- Mar-2011
- Publisher
- SPRINGER
- Citation
- CURRENT MICROBIOLOGY, v.62, no.3, pp 861 - 865
- Pages
- 5
- Journal Title
- CURRENT MICROBIOLOGY
- Volume
- 62
- Number
- 3
- Start Page
- 861
- End Page
- 865
- URI
- https://scholarworks.bwise.kr/cau/handle/2019.sw.cau/21700
- DOI
- 10.1007/s00284-010-9771-6
- ISSN
- 0343-8651
1432-0991
- Abstract
- RNase E (Rne) plays a key role in the processing and degradation of RNA in Escherichia coli. In the genome of Vibrio vulnificus, one open reading frame potentially encodes a protein homologous to E. coli RNase E, designated RNase EV, which N-terminal (1-500 amino acids) has 86.4% amino acid identity to the N-terminal catalytic part of RNase E (N-Rne). Here, we report that both the full-length and the N-terminal part of RNase EV (N-RneV) functionally complement E. coli RNase E and their expression consequently supports normal growth of RNase E-depleted E. coli cells. E. coli cells expressing N-RneV showed copy numbers of ColE1-type plasmid similar to that of E. coli cells expressing N-Rne, indicating in vivo ribonucleolytic activity of N-RneV on RNA I, an antisense regulator of ColE1-type plasmid replication. In vitro cleavage assays further showed that N-RneV has cleavage activity and specificity of RNase E on RNase E-targeted sequence of RNA I (BR13). Our findings suggest that RNase E-like proteins have conserved enzymatic properties that determine substrate specificity across species.
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