Molecular recognition of RhlB and RNase D in the Caulobacter crescentus RNA degradosome
Nucleic Acids Research
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Voss, J. E., Luisi, B., & Hardwick, S. (2014). Molecular recognition of RhlB and RNase D in the Caulobacter crescentus RNA degradosome. Nucleic Acids Research, 42 13294-13305. https://doi.org/10.1093/nar/gku1134
The endoribonuclease RNase E is a key enzyme in RNA metabolism for many bacterial species. In Escherichia coli, RNase E contributes to the majority of RNA turnover and processing events, and the enzyme has been extensively characterized as the central component of the RNA degradosome assembly. A similar RNA degradosome assembly has been described in the α-proteobacterium Caulobacter crescentus, with the interacting partners of RNase E identified as the Kreb's cycle enzyme aconitase, a DEAD-box RNA helicase RhlB and the exoribonuclease polynucleotide phosphorylase. Here we report that an additional degradosome component is the essential exoribonuclease RNase D, and its recognition site within RNase E is identified. We show that, unlike its E. coli counterpart, C. crescentus RhlB interacts directly with a segment of the N-terminal catalytic domain of RNase E. The crystal structure of a portion of C. crescentus RNase E encompassing the helicase-binding region is reported. This structure reveals that an inserted segment in the S1 domain adopts an α-helical conformation, despite being predicted to be natively unstructured. We discuss the implications of these findings for the organization and mechanisms of the RNA degradosome.
Wellcome Trust funding [RG61065 to B.F.L]; Herschel Smith Scholarship [to J.E.V.]. Funding for open access charge: Wellcome Trust [to B.F.L.].
External DOI: https://doi.org/10.1093/nar/gku1134
This record's URL: https://www.repository.cam.ac.uk/handle/1810/246346
Attribution 2.0 UK: England & Wales
Licence URL: http://creativecommons.org/licenses/by/2.0/uk/
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