The basic tilted helix bundle domain of the prolyl isomerase FKBP25 is a novel double-stranded RNA binding module

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dc.contributor.authorDilworth, David
dc.contributor.authorUpadhyay, Santosh K.
dc.contributor.authorBonnafous, Pierre
dc.contributor.authorEdoo, Amiirah Bibi
dc.contributor.authorBourbigot, Sarah
dc.contributor.authorPesek-Jardim, Francy
dc.contributor.authorGudavicius, Geoff
dc.contributor.authorSerpa, Jason J.
dc.contributor.authorPetrotchenko, Evgeniy V.
dc.contributor.authorBorchers, Christoph H.
dc.contributor.authorNelson, Christopher J.
dc.contributor.authorMackereth, Cameron D.
dc.date.accessioned2019-03-21T00:15:11Z
dc.date.available2019-03-21T00:15:11Z
dc.date.copyright2017en_US
dc.date.issued2017
dc.description.abstractProlyl isomerases are defined by a catalytic domain that facilitates the cis–trans interconversion of proline residues. In most cases, additional domains in these enzymes add important biological function, including recruitment to a set of protein substrates. Here, we report that the N-terminal basic tilted helix bundle (BTHB) domain of the human prolyl isomerase FKBP25 confers specific binding to double-stranded RNA (dsRNA). This binding is selective over DNA as well as single-stranded oligonucleotides. We find that FKBP25 RNA-association is required for its nucleolar localization and for the vast majority of its protein interactions, including those with 60S pre-ribosome and early ribosome biogenesis factors. An independent mobility of the BTHB and FKBP catalytic domains supports a model by which the N-terminus of FKBP25 is anchored to regions of dsRNA, whereas the FKBP domain is free to interact with neighboring proteins. Apart from the identification of the BTHB as a new dsRNA-binding module, this domain adds to the growing list of auxiliary functions used by prolyl isomerases to define their primary cellular targets.en_US
dc.description.reviewstatusRevieweden_US
dc.description.scholarlevelFacultyen_US
dc.description.sponsorshipFrench Canada Research Fund [C.J.N. and C.D.M.]; Fondation ARC for Cancer Research [PDF20111204271 to S.K.U.]; Canadian Breast Cancer Foundation BC/Yukon Branch [to C.J.N.]; Discovery Grant and Accelerator Supplement from the Natural Sciences and Engineering Research Council of Canada [to C.J.N.]. Funding for open access charge: Inserm.en_US
dc.identifier.citationDilworth, D.; Upadhyay, S. K.; Bonnafous, P.; Edoo, A. B.; Bourbigot, S.; Pesek- Jardim, F.; … & Mackereth, C. D. (2017). The basic tilted helix bundle domain of the prolyl isomerase FKBP25 is a novel double-stranded RNA binding module. Nucleic Acids Research, 45(20), 11989-12004. DOI: 10.1093/nar/gkx852en_US
dc.identifier.urihttps://doi.org/10.1093/nar/gkx852
dc.identifier.urihttp://hdl.handle.net/1828/10658
dc.language.isoenen_US
dc.publisherNucleic Acids Researchen_US
dc.subjectUVic Genome BC Proteomics Centre
dc.subject.departmentDepartment of Microbiology and Biochemistry
dc.subject.departmentDepartment of Biochemistry and Microbiology
dc.titleThe basic tilted helix bundle domain of the prolyl isomerase FKBP25 is a novel double-stranded RNA binding moduleen_US
dc.typeArticleen_US

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