Stabilization of Nucleosomes by Histone Tails and by FACT Revealed by SpFRET Microscopy

Overview

Journal Cancers (Basel)

Publisher MDPI

Specialty Oncology

Date 2017 Jan 10

PMID 28067802

Citations 21

Authors

Maria E Valieva

Nadezhda S Gerasimova

Kseniya S Kudryashova

Anastasia L Kozlova

Mikhail P Kirpichnikov

Qi Hu

Maria Victoria Botuyan

Georges Mer

Alexey V Feofanov

Vasily M Studitsky

Affiliations

Soon will be listed here.

Abstract

A correct chromatin structure is important for cell viability and is tightly regulated by numerous factors. Human protein complex FACT (facilitates chromatin transcription) is an essential factor involved in chromatin transcription and cancer development. Here FACT-dependent changes in the structure of single nucleosomes were studied with single-particle Förster resonance energy transfer (spFRET) microscopy using nucleosomes labeled with a donor-acceptor pair of fluorophores, which were attached to the adjacent gyres of DNA near the contact between H2A-H2B dimers. Human FACT and its version without the C-terminal domain (CTD) and the high mobility group (HMG) domain of the structure-specific recognition protein 1 (SSRP1) subunit did not change the structure of the nucleosomes, while FACT without the acidic C-terminal domains of the suppressor of Ty 16 (Spt16) and the SSRP1 subunits caused nucleosome aggregation. Proteolytic removal of histone tails significantly disturbed the nucleosome structure, inducing partial unwrapping of nucleosomal DNA. Human FACT reduced DNA unwrapping and stabilized the structure of tailless nucleosomes. CTD and/or HMG domains of SSRP1 are required for this FACT activity. In contrast, previously it has been shown that yeast FACT unfolds (reorganizes) nucleosomes using the CTD domain of SSRP1-like Pol I-binding protein 3 subunit (Pob3). Thus, yeast and human FACT complexes likely utilize the same domains for nucleosome reorganization and stabilization, respectively, and these processes are mechanistically similar.

Citing Articles

Transcriptional regulation of FACT involves Coordination of chromatin accessibility and CTCF binding.

Wang P, Fan N, Yang W, Cao P, Liu G, Zhao Q J Biol Chem. 2023; 300(1):105538.

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Interactions of Nucleosomes with Acidic Patch-Binding Peptides: A Combined Structural Bioinformatics, Molecular Modeling, Fluorescence Polarization, and Single-Molecule FRET Study.

Oleinikov P, Fedulova A, Armeev G, Motorin N, Singh-Palchevskaia L, Sivkina A Int J Mol Sci. 2023; 24(20).

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Structure and Dynamics of Compact Dinucleosomes: Analysis by Electron Microscopy and spFRET.

Stefanova M, Volokh O, Chertkov O, Armeev G, Shaytan A, Feofanov A Int J Mol Sci. 2023; 24(15).

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Structural Transition of the Nucleosome during Transcription Elongation.

Kujirai T, Ehara H, Sekine S, Kurumizaka H Cells. 2023; 12(10).

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Opposing Roles of FACT for Euchromatin and Heterochromatin in Yeast.

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