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dc.contributor.authorCamacho, Inês S; orcid: 0000-0001-9351-8981
dc.contributor.authorBlack, Rachelle; orcid: 0000-0002-7067-2385
dc.contributor.authorHeyes, Derren J; orcid: 0000-0002-7453-1571
dc.contributor.authorJohannissen, Linus O; orcid: 0000-0002-0916-9094
dc.contributor.authorRamakers, Lennart A I
dc.contributor.authorBellina, Bruno
dc.contributor.authorBarran, Perdita E; orcid: 0000-0002-7720-586X
dc.contributor.authorHay, Sam; orcid: 0000-0003-3274-0938
dc.contributor.authorJones, Alex R; orcid: 0000-0001-6021-7824
dc.date.accessioned2021-07-20T13:49:51Z
dc.date.available2021-07-20T13:49:51Z
dc.date.issued2021-05-05
dc.identifierpubmed: 34221314
dc.identifierdoi: 10.1039/d1sc00522g
dc.identifierpii: d1sc00522g
dc.identifierpmc: PMC8221060
dc.identifier.citationChemical science, volume 12, issue 24, page 8333-8341
dc.identifier.urihttp://hdl.handle.net/10034/625310
dc.descriptionFrom PubMed via Jisc Publications Router
dc.descriptionPublication status: epublish
dc.description.abstractOrganisms across the natural world respond to their environment through the action of photoreceptor proteins. The vitamin B -dependent photoreceptor, CarH, is a bacterial transcriptional regulator that controls the biosynthesis of carotenoids to protect against photo-oxidative stress. The binding of B to CarH monomers in the dark results in the formation of a homo-tetramer that complexes with DNA; B photochemistry results in tetramer dissociation, releasing DNA for transcription. Although the details of the response of CarH to light are beginning to emerge, the biophysical mechanism of B -binding in the dark and how this drives domain assembly is poorly understood. Here - using a combination of molecular dynamics simulations, native ion mobility mass spectrometry and time-resolved spectroscopy - we reveal a complex picture that varies depending on the availability of B . When B is in excess, its binding drives structural changes in CarH monomers that result in the formation of head-to-tail dimers. The structural changes that accompany these steps mean that they are rate-limiting. The dimers then rapidly combine to form tetramers. Strikingly, when B is scarcer, as is likely in nature, tetramers with native-like structures can form without a B complement to each monomer, with only one apparently required per head-to-tail dimer. We thus show how a bulky chromophore such as B shapes protein/protein interactions and in turn function, and how a protein can adapt to a sub-optimal availability of resources. This nuanced picture should help guide the engineering of B -dependent photoreceptors as light-activated tools for biomedical applications. [Abstract copyright: This journal is © The Royal Society of Chemistry.]
dc.languageeng
dc.sourcepissn: 2041-6520
dc.titleInterplay between chromophore binding and domain assembly by the B
dc.typearticle
dc.date.updated2021-07-20T13:49:51Z


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