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Sci Rep. 2017 Jun 19;7(1):3795. doi: 10.1038/s41598-017-04194-7.

Basic surface features of nuclear FKBPs facilitate chromatin binding.

Author information

1
Department of Biochemistry & Microbiology, University of Victoria, Victoria, BC V8W 3P6, Canada.
2
Univ. Bordeaux, Inserm, CNRS, ARNA Laboratory, U1212, UMR 5320, Institut Européen de Chimie et Biologie, 2 rue Robert Escarpit, 33076, Pessac, France.
3
Chromatin Structure and Evolution (Chromevol) Group, Department of Biological Sciences, Florida International University, North Miami, FL, USA.
4
MRC London Institute of Medical Sciences (LMS), Du Cane Road, London, W12 0NN, UK.
5
Institute of Clinical Sciences (ICS), Faculty of Medicine, Imperial College London, Du Cane Road, London, W12 0NN, UK.
6
Department of Biochemistry & Microbiology, University of Victoria, Victoria, BC V8W 3P6, Canada. cjn@uvic.ca.

Abstract

The nucleoplasmin family of histone chaperones is identified by a pentamer-forming domain and multiple acidic tracts that mediate histone binding and chaperone activity. Within this family, a novel domain organization was recently discovered that consists of an N-terminal nucleoplasmin-like (NPL) domain and a C-terminal FKBP peptidyl-proline isomerase domain. Saccharomyces cerevisiae Fpr4 is one such protein. Here we report that in addition to its known histone prolyl isomerase activities, the Fpr4 FKBP domain binds to nucleosomes and nucleosome arrays in vitro. This ability is mediated by a collection of basic patches that enable the enzyme to stably associate with linker DNA. The interaction of the Fpr4 FKBP with recombinant chromatin complexes condenses nucleosome arrays independently of its catalytic activity. Based on phylogenetic comparisons we propose that the chromatin binding ability of 'basic' FKBPs is shared amongst related orthologues present in fungi, plants, and insects. Thus, a subclass of FKBP prolyl isomerase enzymes is recruited to linker regions of chromatin.

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