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Nucleic Acids Res. 2017 Nov 16;45(20):11989-12004. doi: 10.1093/nar/gkx852.

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

Author information

1
Dept. of Biochemistry and Microbiology, University of Victoria, Victoria, BC V8W 3P6, Canada.
2
Univ. Bordeaux, Institut Européen de Chimie et Biologie, 2 rue Robert Escarpit, F-33607 Pessac, France.
3
Inserm U1212, CNRS UMR 5320, ARNA Laboratory, Univ. Bordeaux, 146 rue Léo Saignat, F-33076 Bordeaux, France.
4
CSIR-Institute of Genomics and Integrative Biology, New Delhi 110020, India.
5
University of Victoria Genome BC Proteomics Centre, Vancouver Island Technology Park, Victoria, BC V8Z 7X8, Canada.

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.

PMID:
29036638
PMCID:
PMC5714180
DOI:
10.1093/nar/gkx852
[Indexed for MEDLINE]
Free PMC Article

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