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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Acknowledgments
We thank Dr. Stanley N. Cohen for providing us with monoclonal antibodies to Rne and polyclonal antibodies to S1.
Funding
This research was supported by the Chung-Ang University Research Grants in 2010.
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Lee, M., Yeom, JH., Jeon, C.O. et al. Studies on a Vibrio vulnificus Functional Ortholog of Escherichia coli RNase E Imply a Conserved Function of RNase E-like Enzymes in Bacteria. Curr Microbiol 62, 861–865 (2011). https://doi.org/10.1007/s00284-010-9771-6
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DOI: https://doi.org/10.1007/s00284-010-9771-6