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

Date

2017

Authors

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

Journal Title

Journal ISSN

Volume Title

Publisher

Nucleic Acids Research

Abstract

Prolyl 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.

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Citation

Dilworth, 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/gkx852