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

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 basi...

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Bibliographic Details
Published in:	Nucleic acids research Vol. 45; no. 20; pp. 11989 - 12004
Main 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, Nelson, Christopher J, Mackereth, Cameron D
Format:	Journal Article
Language:	English
Published:	England Oxford University Press 16-11-2017
Subjects:	Base Sequence Blotting, Western Catalytic Domain Cell Line, Tumor HEK293 Cells Humans Microscopy, Confocal Models, Molecular Nucleic Acid Conformation Protein Binding Protein Domains Protein Structure, Secondary Ribosomes - genetics Ribosomes - metabolism RNA, Double-Stranded - chemistry RNA, Double-Stranded - genetics RNA, Double-Stranded - metabolism Structural Biology Tacrolimus Binding Proteins - chemistry Tacrolimus Binding Proteins - genetics Tacrolimus Binding Proteins - metabolism
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Summary:	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.
Bibliography:	ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 These authors contributed equally to this work as first authors.
ISSN:	0305-1048 1362-4962
DOI:	10.1093/nar/gkx852