Analysis of the natively unstructured RNA/protein-recognition core in the Escherichia coli RNA degradosome and its interactions with regulatory RNA/Hfq complexes.
View / Open Files
Authors
Bruce, Heather A
Broadhurst, Bill
Martin, Esther
Shkumatov, Alexander V
Publication Date
2018-01Journal Title
Nucleic acids research
ISSN
0305-1048
Publisher
Oxford University Press
Volume
46
Issue
1
Pages
387-402
Language
eng
Type
Article
This Version
VoR
Physical Medium
Print
Metadata
Show full item recordCitation
Bruce, H. A., Du, D., Matak Vinkovic, D., Bandyra, K., Broadhurst, B., Martin, E., Sobott, F., et al. (2018). Analysis of the natively unstructured RNA/protein-recognition core in the Escherichia coli RNA degradosome and its interactions with regulatory RNA/Hfq complexes.. Nucleic acids research, 46 (1), 387-402. https://doi.org/10.1093/nar/gkx1083
Abstract
The RNA degradosome is a multi-enzyme assembly that plays a central role in the RNA metabolism of Escherichia coli and numerous other bacterial species including pathogens. At the core of the assembly is the endoribonuclease RNase E, one of the largest E. coli proteins and also one that bears the greatest region predicted to be natively unstructured. The extensive unstructured region, situated in the C-terminal half of RNase E, is punctuated with conserved short linear motifs that recruit partner proteins, direct RNA interactions, and enable association with the cytoplasmic membrane. We have structurally characterised a subassembly of the degradosome - comprising a 248-residue segment of the natively unstructured part of RNase E, the DEAD-box helicase RhlB, and the glycolytic enzyme enolase – and provide evidence that it serves as a flexible recognition centre that can co-recruit small regulatory RNA (sRNA) and the RNA chaperone Hfq. Our results support a model in which the degradosome captures substrates and regulatory RNAs through the recognition centre, facilitates pairing to cognate transcripts, and presents the target to the ribonuclease active sites of the greater assembly for cooperative degradation or processing.
Keywords
Multienzyme Complexes, Endoribonucleases, Polyribonucleotide Nucleotidyltransferase, RNA Helicases, Escherichia coli Proteins, Host Factor 1 Protein, RNA, Bacterial, Crystallography, X-Ray, Binding Sites, Nucleic Acid Conformation, Protein Binding, Models, Molecular, Protein Domains
Sponsorship
Wellcome Trust (094229/Z/10/Z)
WELLCOME TRUST (200873/Z/16/Z)
Identifiers
External DOI: https://doi.org/10.1093/nar/gkx1083
This record's URL: https://www.repository.cam.ac.uk/handle/1810/276469
Recommended or similar items
The following licence files are associated with this item: