Crystal Structure of E. coli RNase E and RNA Degradation Mechanism
Author Information
Author(s): Koslover Daniel J., Callaghan Anastasia J., Marcaida Maria J., Garman Elspeth F., Martick Monika, Scott William G., Luisi Ben F.
Primary Institution: Department of Biochemistry, University of Cambridge
Hypothesis
What is the mechanism of RNA recognition and cleavage by RNase E?
Conclusion
The study reveals a conformational change in RNase E that explains its preference for substrates with a 5′-monophosphate.
Supporting Evidence
- RNase E is essential for mRNA degradation in E. coli.
- The crystal structure was determined at a resolution of 3.3 Å.
- Conformational changes in RNase E are crucial for its catalytic activity.
- Substrates with a 5′-monophosphate are cleaved more efficiently than those with other terminal modifications.
Takeaway
RNase E is like a pair of scissors for RNA, and it works best when the RNA has a special end that helps it fit better.
Methodology
The crystal structure of the RNase E apoprotein was solved using X-ray crystallography.
Limitations
The electron density maps were of poor quality for some residues, affecting the confidence in certain structural interpretations.
Digital Object Identifier (DOI)
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