Stabilization of nucleosomes by histone tails and by FACT revealed by spFRET microscopy

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

Research output: Contribution to journalArticle

13 Citations (Scopus)

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.

Original languageEnglish (US)
Article number3
JournalCancers
Volume9
Issue number1
DOIs
StatePublished - Jan 1 2017

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Nucleosomes
Energy Transfer
Histones
Chromatin
Tail
Microscopy
Protein Subunits
DNA
Yeasts
Cell Survival
Carrier Proteins
Proteins

Keywords

  • Facilitates chromatin transcription
  • FACT
  • Nucleosome
  • Spt16
  • SSRP1

ASJC Scopus subject areas

  • Oncology
  • Cancer Research

Cite this

Valieva, M. E., Gerasimova, N. S., Kudryashova, K. S., Kozlova, A. L., Kirpichnikov, M. P., Hu, Q., ... Studitsky, V. M. (2017). Stabilization of nucleosomes by histone tails and by FACT revealed by spFRET microscopy. Cancers, 9(1), [3]. https://doi.org/10.3390/cancers9010003

Stabilization of nucleosomes by histone tails and by FACT revealed by spFRET microscopy. / Valieva, Maria E.; Gerasimova, Nadezhda S.; Kudryashova, Kseniya S.; Kozlova, Anastasia L.; Kirpichnikov, Mikhail P.; Hu, Qi; Botuyan, Maria Victoria; Mer, Georges; Feofanov, Alexey V.; Studitsky, Vasily M.

In: Cancers, Vol. 9, No. 1, 3, 01.01.2017.

Research output: Contribution to journalArticle

Valieva, ME, Gerasimova, NS, Kudryashova, KS, Kozlova, AL, Kirpichnikov, MP, Hu, Q, Botuyan, MV, Mer, G, Feofanov, AV & Studitsky, VM 2017, 'Stabilization of nucleosomes by histone tails and by FACT revealed by spFRET microscopy', Cancers, vol. 9, no. 1, 3. https://doi.org/10.3390/cancers9010003
Valieva ME, Gerasimova NS, Kudryashova KS, Kozlova AL, Kirpichnikov MP, Hu Q et al. Stabilization of nucleosomes by histone tails and by FACT revealed by spFRET microscopy. Cancers. 2017 Jan 1;9(1). 3. https://doi.org/10.3390/cancers9010003
Valieva, Maria E. ; Gerasimova, Nadezhda S. ; Kudryashova, Kseniya S. ; Kozlova, Anastasia L. ; Kirpichnikov, Mikhail P. ; Hu, Qi ; Botuyan, Maria Victoria ; Mer, Georges ; Feofanov, Alexey V. ; Studitsky, Vasily M. / Stabilization of nucleosomes by histone tails and by FACT revealed by spFRET microscopy. In: Cancers. 2017 ; Vol. 9, No. 1.
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