Basic surface features of nuclear FKBPs facilitate chromatin binding

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...

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Main Authors:	Andrew Leung, Francy-Pesek Jardim, Neda Savic, Yoan R. Monneau, Rodrigo González-Romero, Geoff Gudavicius, Jose M. Eirin-Lopez, Till Bartke, Cameron D. Mackereth, Juan Ausió, Christopher J. Nelson
Format:	article
Language:	EN
Published:	Nature Portfolio 2017
Subjects:	Medicine R Science Q
Online Access:	https://doaj.org/article/204654fcae6b4d88805631883411b262
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spelling	oai:doaj.org-article:204654fcae6b4d88805631883411b2622021-12-02T12:30:13ZBasic surface features of nuclear FKBPs facilitate chromatin binding10.1038/s41598-017-04194-72045-2322https://doaj.org/article/204654fcae6b4d88805631883411b2622017-06-01T00:00:00Zhttps://doi.org/10.1038/s41598-017-04194-7https://doaj.org/toc/2045-2322Abstract 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.Andrew LeungFrancy-Pesek JardimNeda SavicYoan R. MonneauRodrigo González-RomeroGeoff GudaviciusJose M. Eirin-LopezTill BartkeCameron D. MackerethJuan AusióChristopher J. NelsonNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 7, Iss 1, Pp 1-10 (2017)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Andrew Leung Francy-Pesek Jardim Neda Savic Yoan R. Monneau Rodrigo González-Romero Geoff Gudavicius Jose M. Eirin-Lopez Till Bartke Cameron D. Mackereth Juan Ausió Christopher J. Nelson Basic surface features of nuclear FKBPs facilitate chromatin binding
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.
format	article
author	Andrew Leung Francy-Pesek Jardim Neda Savic Yoan R. Monneau Rodrigo González-Romero Geoff Gudavicius Jose M. Eirin-Lopez Till Bartke Cameron D. Mackereth Juan Ausió Christopher J. Nelson
author_facet	Andrew Leung Francy-Pesek Jardim Neda Savic Yoan R. Monneau Rodrigo González-Romero Geoff Gudavicius Jose M. Eirin-Lopez Till Bartke Cameron D. Mackereth Juan Ausió Christopher J. Nelson
author_sort	Andrew Leung
title	Basic surface features of nuclear FKBPs facilitate chromatin binding
title_short	Basic surface features of nuclear FKBPs facilitate chromatin binding
title_full	Basic surface features of nuclear FKBPs facilitate chromatin binding
title_fullStr	Basic surface features of nuclear FKBPs facilitate chromatin binding
title_full_unstemmed	Basic surface features of nuclear FKBPs facilitate chromatin binding
title_sort	basic surface features of nuclear fkbps facilitate chromatin binding
publisher	Nature Portfolio
publishDate	2017
url	https://doaj.org/article/204654fcae6b4d88805631883411b262
work_keys_str_mv	AT andrewleung basicsurfacefeaturesofnuclearfkbpsfacilitatechromatinbinding AT francypesekjardim basicsurfacefeaturesofnuclearfkbpsfacilitatechromatinbinding AT nedasavic basicsurfacefeaturesofnuclearfkbpsfacilitatechromatinbinding AT yoanrmonneau basicsurfacefeaturesofnuclearfkbpsfacilitatechromatinbinding AT rodrigogonzalezromero basicsurfacefeaturesofnuclearfkbpsfacilitatechromatinbinding AT geoffgudavicius basicsurfacefeaturesofnuclearfkbpsfacilitatechromatinbinding AT josemeirinlopez basicsurfacefeaturesofnuclearfkbpsfacilitatechromatinbinding AT tillbartke basicsurfacefeaturesofnuclearfkbpsfacilitatechromatinbinding AT camerondmackereth basicsurfacefeaturesofnuclearfkbpsfacilitatechromatinbinding AT juanausio basicsurfacefeaturesofnuclearfkbpsfacilitatechromatinbinding AT christopherjnelson basicsurfacefeaturesofnuclearfkbpsfacilitatechromatinbinding
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Basic surface features of nuclear FKBPs facilitate chromatin binding

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