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

David Dilworth, Santosh K. Upadhyay, Pierre Bonnafous, Amiirah Bibi Edoo, Sarah Bourbigot, Francy Pesek-Jardim, Geoff Gudavicius, Jason J. Serpa, Evgeniy V. Petrotchenko, Christoph H. Borchers, Christopher J. Nelson, Cameron D. MacKereth

Research output: Contribution to journalArticlepeer-review

9 Citations (Scopus)

Abstract

Prolyl isomerases are defined by a catalytic domain that facilitates the cis-transinterconversion 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 helix tilted 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.

Original languageEnglish
Pages (from-to)1-16
Number of pages16
JournalNucleic Acids Research
Volume45
Issue number20
DOIs
Publication statusPublished - Nov 2017
Externally publishedYes

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