Basic surface features of nuclear FKBPs facilitate chromatin binding
| dc.contributor.author | Leung, Andrew | |
| dc.contributor.author | Jardim, Francy-Pesek | |
| dc.contributor.author | Savic, Neda | |
| dc.contributor.author | Monneau, Yoan R. | |
| dc.contributor.author | González-Romero, Rodrigo | |
| dc.contributor.author | Gudavicius, Geoff | |
| dc.contributor.author | Eirin-Lopez, Jose M. | |
| dc.contributor.author | Bartke, Till | |
| dc.contributor.author | Mackereth, Cameron D. | |
| dc.contributor.author | Ausió, Juan | |
| dc.contributor.author | Nelson, Christopher J. | |
| dc.date.accessioned | 2018-08-27T14:37:24Z | |
| dc.date.available | 2018-08-27T14:37:24Z | |
| dc.date.copyright | 2017 | en_US |
| dc.date.issued | 2017 | |
| dc.description.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. | en_US |
| dc.description.reviewstatus | Reviewed | en_US |
| dc.description.scholarlevel | Faculty | en_US |
| dc.description.sponsorship | This work was supported by a Discovery Grant and an Accelerator Supplement from the Natural Sciences and Engineering Research Council of Canada (NSERC) awarded to C.J.N.; an NSERC Discovery Grant to J.A. and a grant from the Biomolecular Sciences Institute (800005997) and the College of Arts, Sciences and Education at Florida International University to J.M.E.-L. | en_US |
| dc.identifier.citation | Leung, A.; Jardim, F.; Savic, N.; Monneau, Y.R.; González-Romero, R.; Gudavicius, G.; … & Nelson, C.J. (2017). Basic surface features of nuclear FKBPs facilitate chromatin binding. Scientific Reports, 7, article 3795. doi: /10.1038/s41598-017- 04194-7 | en_US |
| dc.identifier.uri | https://doi.org/10.1038/s41598-017-04194-7 | |
| dc.identifier.uri | http://hdl.handle.net/1828/9959 | |
| dc.language.iso | en | en_US |
| dc.publisher | Scientific Reports | en_US |
| dc.subject.department | Department of Biochemistry and Microbiology | |
| dc.title | Basic surface features of nuclear FKBPs facilitate chromatin binding | en_US |
| dc.type | Article | en_US |