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Basic surface features of nuclear FKBPs facilitate chromatin binding.

Andrew Leung1, Francy-Pesek Jardim1, Neda Savic1

  • 1Department of Biochemistry & Microbiology, University of Victoria, Victoria, BC V8W 3P6, Canada.

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|June 21, 2017
PubMed
Summary
This summary is machine-generated.

The FKBP domain of Saccharomyces cerevisiae Fpr4 binds to nucleosomes and chromatin. This interaction, mediated by basic patches, condenses nucleosome arrays, suggesting a role for FKBP prolyl isomerases in chromatin regulation.

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Area of Science:

  • Molecular Biology
  • Chromatin Biology
  • Protein Biochemistry

Background:

  • The nucleoplasmin family are histone chaperones characterized by pentamer-forming and acidic domains.
  • A novel domain organization includes an N-terminal nucleoplasmin-like (NPL) domain and a C-terminal FKBP peptidyl-proline isomerase domain.
  • Saccharomyces cerevisiae Fpr4 exemplifies this novel domain organization.

Purpose of the Study:

  • To investigate the non-catalytic functions of the Fpr4 FKBP domain.
  • To determine if the Fpr4 FKBP domain interacts with chromatin structures.
  • To explore the implications of this interaction for chromatin organization.

Main Methods:

  • In vitro binding assays using recombinant chromatin complexes and nucleosome arrays.
  • Biochemical characterization of Fpr4 FKBP domain interactions.
  • Phylogenetic analysis of related FKBP proteins.

Main Results:

  • The Fpr4 FKBP domain exhibits binding to nucleosomes and nucleosome arrays.
  • Basic patches on the Fpr4 FKBP domain mediate stable association with linker DNA.
  • Fpr4 FKBP interaction with chromatin condensates nucleosome arrays independently of its isomerase activity.

Conclusions:

  • A subclass of FKBP prolyl isomerase enzymes possesses chromatin-binding capabilities.
  • These enzymes are recruited to the linker regions of chromatin.
  • This suggests a conserved role for 'basic' FKBPs in chromatin regulation across fungi, plants, and insects.