Substrate Recognition and Autoinhibition in the Central Ribonuclease RNase E.
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Publication Date
2018-10-18Journal Title
Mol Cell
ISSN
1097-2765
Publisher
Elsevier BV
Volume
72
Issue
2
Pages
275-285.e4
Language
eng
Type
Article
Physical Medium
Print-Electronic
Metadata
Show full item recordCitation
Bandyra, K., Wandzik, J. M., & Luisi, B. (2018). Substrate Recognition and Autoinhibition in the Central Ribonuclease RNase E.. Mol Cell, 72 (2), 275-285.e4. https://doi.org/10.1016/j.molcel.2018.08.039
Abstract
The endoribonuclease RNase E is a principal factor in RNA turnover and processing that helps to exercise fine control of gene expression in bacteria. While its catalytic activity can be strongly influenced by the chemical identity of the 5' end of RNA substrates, the enzyme can also cleave numerous substrates irrespective of the chemistry of their 5' ends through a mechanism that has remained largely unexplained. We report structural and functional data illuminating details of both operational modes. Our crystal structure of RNase E in complex with the sRNA RprA reveals a duplex recognition site that saddles an inter-protomer surface to help present substrates for cleavage. Our data also reveal an autoinhibitory pocket that modulates the overall activity of the ribonuclease. Taking these findings together, we propose how RNase E uses versatile modes of RNA recognition to achieve optimal activity and specificity.
Keywords
Escherichia coli, Endoribonucleases, Escherichia coli Proteins, Protein Subunits, RNA, RNA, Bacterial, Sequence Alignment, Gene Expression Regulation, Bacterial, Amino Acid Sequence, Substrate Specificity, Catalysis
Sponsorship
Wellcome Trust
Funder references
Wellcome Trust (200873/Z/16/Z)
Identifiers
External DOI: https://doi.org/10.1016/j.molcel.2018.08.039
This record's URL: https://www.repository.cam.ac.uk/handle/1810/284687
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