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Article

Hmo1 Protein Affects the Nucleosome Structure and Supports the Nucleosome Reorganization Activity of Yeast FACT

by
Daria K. Malinina
1,
Anastasiia L. Sivkina
1,
Anna N. Korovina
1,
Laura L. McCullough
2,
Tim Formosa
2,
Mikhail P. Kirpichnikov
1,3,
Vasily M. Studitsky
1,4,* and
Alexey V. Feofanov
1,3,*
1
Biology Faculty, Lomonosov Moscow State University, 119992 Moscow, Russia
2
Department of Biochemistry, University of Utah School of Medicine, Salt Lake City, UT 84132, USA
3
Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, 117997 Moscow, Russia
4
Fox Chase Cancer Center, Philadelphia, PA 19111, USA
*
Authors to whom correspondence should be addressed.
Cells 2022, 11(19), 2931; https://doi.org/10.3390/cells11192931
Submission received: 16 August 2022 / Revised: 6 September 2022 / Accepted: 15 September 2022 / Published: 20 September 2022
(This article belongs to the Special Issue Nucleosome Structure, Dynamics and Interactions)
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Abstract

Yeast Hmo1 is a high mobility group B (HMGB) protein that participates in the transcription of ribosomal protein genes and rDNA, and also stimulates the activities of some ATP-dependent remodelers. Hmo1 binds both DNA and nucleosomes and has been proposed to be a functional yeast analog of mammalian linker histones. We used EMSA and single particle Förster resonance energy transfer (spFRET) microscopy to characterize the effects of Hmo1 on nucleosomes alone and with the histone chaperone FACT. Hmo1 induced a significant increase in the distance between the DNA gyres across the nucleosomal core, and also caused the separation of linker segments. This was opposite to the effect of the linker histone H1, which enhanced the proximity of linkers. Similar to Nhp6, another HMGB factor, Hmo1, was able to support large-scale, ATP-independent, reversible unfolding of nucleosomes by FACT in the spFRET assay and partially support FACT function in vivo. However, unlike Hmo1, Nhp6 alone does not affect nucleosome structure. These results suggest physiological roles for Hmo1 that are distinct from Nhp6 and possibly from other HMGB factors and linker histones, such as H1.
Keywords: nucleosome; Hmo1; FACT; high mobility group B protein; H1 histone; spFRET; EMSA nucleosome; Hmo1; FACT; high mobility group B protein; H1 histone; spFRET; EMSA

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MDPI and ACS Style

Malinina, D.K.; Sivkina, A.L.; Korovina, A.N.; McCullough, L.L.; Formosa, T.; Kirpichnikov, M.P.; Studitsky, V.M.; Feofanov, A.V. Hmo1 Protein Affects the Nucleosome Structure and Supports the Nucleosome Reorganization Activity of Yeast FACT. Cells 2022, 11, 2931. https://doi.org/10.3390/cells11192931

AMA Style

Malinina DK, Sivkina AL, Korovina AN, McCullough LL, Formosa T, Kirpichnikov MP, Studitsky VM, Feofanov AV. Hmo1 Protein Affects the Nucleosome Structure and Supports the Nucleosome Reorganization Activity of Yeast FACT. Cells. 2022; 11(19):2931. https://doi.org/10.3390/cells11192931

Chicago/Turabian Style

Malinina, Daria K., Anastasiia L. Sivkina, Anna N. Korovina, Laura L. McCullough, Tim Formosa, Mikhail P. Kirpichnikov, Vasily M. Studitsky, and Alexey V. Feofanov. 2022. "Hmo1 Protein Affects the Nucleosome Structure and Supports the Nucleosome Reorganization Activity of Yeast FACT" Cells 11, no. 19: 2931. https://doi.org/10.3390/cells11192931

APA Style

Malinina, D. K., Sivkina, A. L., Korovina, A. N., McCullough, L. L., Formosa, T., Kirpichnikov, M. P., Studitsky, V. M., & Feofanov, A. V. (2022). Hmo1 Protein Affects the Nucleosome Structure and Supports the Nucleosome Reorganization Activity of Yeast FACT. Cells, 11(19), 2931. https://doi.org/10.3390/cells11192931

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