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Structural plasticity of D3-D14 ubiquitin ligase in strigolactone signalling.

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cam.issuedOnline2018-11-21
dc.contributor.authorShabek, Nitzan
dc.contributor.authorTicchiarelli, Fabrizio
dc.contributor.authorMao, Haibin
dc.contributor.authorHinds, Thomas R
dc.contributor.authorLeyser, Ottoline
dc.contributor.authorZheng, Ning
dc.contributor.orcidLeyser, Ottoline [0000-0003-2161-3829]
dc.date.accessioned2018-12-12T00:31:22Z
dc.date.available2018-12-12T00:31:22Z
dc.date.issued2018-11
dc.description.abstractThe strigolactones, a class of plant hormones, regulate many aspects of plant physiology. In the inhibition of shoot branching, the α/β hydrolase D14-which metabolizes strigolactone-interacts with the F-box protein D3 to ubiquitinate and degrade the transcription repressor D53. Despite the fact that multiple modes of interaction between D14 and strigolactone have recently been determined, how the hydrolase functions with D3 to mediate hormone-dependent D53 ubiquitination remains unknown. Here we show that D3 has a C-terminal α-helix that can switch between two conformational states. The engaged form of this α-helix facilitates the binding of D3 and D14 with a hydrolysed strigolactone intermediate, whereas the dislodged form can recognize unmodified D14 in an open conformation and inhibits its enzymatic activity. The D3 C-terminal α-helix enables D14 to recruit D53 in a strigolactone-dependent manner, which in turn activates the hydrolase. By revealing the structural plasticity of the SCFD3-D14 ubiquitin ligase, our results suggest a mechanism by which the E3 coordinates strigolactone signalling and metabolism.
dc.description.sponsorshipGatsby Charitable Foundation
dc.format.mediumPrint-Electronic
dc.identifier.doi10.17863/CAM.34020
dc.identifier.eissn1476-4687
dc.identifier.issn0028-0836
dc.identifier.urihttps://www.repository.cam.ac.uk/handle/1810/286713
dc.languageeng
dc.language.isoeng
dc.publisherSpringer Science and Business Media LLC
dc.publisher.urlhttp://dx.doi.org/10.1038/s41586-018-0743-5
dc.subjectHeterocyclic Compounds, 3-Ring
dc.subjectLactones
dc.subjectModels, Molecular
dc.subjectMultienzyme Complexes
dc.subjectOryza
dc.subjectPlant Growth Regulators
dc.subjectPlant Proteins
dc.subjectProtein Binding
dc.subjectProtein Structure, Secondary
dc.subjectSKP Cullin F-Box Protein Ligases
dc.subjectSignal Transduction
dc.subjectStructure-Activity Relationship
dc.subjectUbiquitin
dc.subjectUbiquitination
dc.titleStructural plasticity of D3-D14 ubiquitin ligase in strigolactone signalling.
dc.typeArticle
dcterms.dateAccepted2018-10-05
prism.endingPage656
prism.issueIdentifier7733
prism.publicationDate2018
prism.publicationNameNature
prism.startingPage652
prism.volume563
pubs.funder-project-idGatsby Charitable Foundation (GAT3395/GL)
pubs.funder-project-idEuropean Research Council (294514)
rioxxterms.licenseref.startdate2018-11-21
rioxxterms.licenseref.urihttp://www.rioxx.net/licenses/all-rights-reserved
rioxxterms.typeJournal Article/Review
rioxxterms.versionAM
rioxxterms.versionofrecord10.1038/s41586-018-0743-5

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