Melting calorimetry of rat liver nuclei in the presence of magnesium ions
- Authors: Kolomijtseva G.Y.1, Prusov A.N1, Kolomijtseva E.A2, Smirnova T.A1,3
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Affiliations:
- Belozersky Institute of Physico-Chemical Biology, Lomonosov Moscow State University
- MIREA - Russian Technological University
- All-Russian Research Institute of Agricultural Biotechnology
- Issue: Vol 68, No 2 (2023)
- Pages: 349-359
- Section: Articles
- URL: https://journals.rcsi.science/0006-3029/article/view/144432
- DOI: https://doi.org/10.31857/S000630292302014X
- EDN: https://elibrary.ru/CBBIGP
- ID: 144432
Cite item
Abstract
Differential scanning calorimetry was used to determine thermodynamic parameters of decondensation of intranuclear rat liver chromatin was induced by a decrease in the concentration of magnesium ions from 5 mM to 0 mM. The process of chromatin melting in the temperature range of 70-100°C occurs in the following order: melting of core-histones, melting of relaxed DNA, and melting of topologically constrained DNA. It was found that Tm and Д H of individual peaks also depend on the concentration of Mg2+ ions in the buffer. In nuclei with condensed chromatin, Mg2+ ions at a concentration of 5 mM increased significantly the Tm of core histones (by ~7°C), as compared to that in unfolded chromatin but at the same time lowered the Tm of nuclear DNA both in the relaxed and constrained state (by ~2.5°С and ~7.5°С, respectively). In the presence of Mg2+ ions, melting enthalpy for peaks increased significantly. At the same time, a decrease in molecular weights of intranuclear DNA levels out a stabilizing effect of Mg2+ ions on core histones. A rise in the concentration of Mg2+ ions above 5 mM leads to the appearance of a new peak with Tm above 100°С, which probably reflects the thermal behavior of some Mg-induced aggregates. Possible mechanisms underlying thermal behavior of chromatin inside the nucleus are discussed.
About the authors
G. Ya Kolomijtseva
Belozersky Institute of Physico-Chemical Biology, Lomonosov Moscow State UniversityMoscow, Russia
A. N Prusov
Belozersky Institute of Physico-Chemical Biology, Lomonosov Moscow State University
Email: prusov@belozersky.msu.ru
Moscow, Russia
E. A Kolomijtseva
MIREA - Russian Technological UniversityMoscow, Russia
T. A Smirnova
Belozersky Institute of Physico-Chemical Biology, Lomonosov Moscow State University;All-Russian Research Institute of Agricultural BiotechnologyMoscow, Russia
References
- E. I. Prieto and K. Maeshima, Essays Biochem., 63 (1), 133 (2019).
- J. R. Daban, Biochemistry, 39, 3861 (2000).
- G. Li and D. Reinberg, Curr. Opin. Genet. Dev., 21, 175 (2011).
- J. C. Hansen, Ann. Rev. Biophys. Biomol. Struct., 31, 361 (2002).
- В. Ю. Поляков, О. В. Зацепина, И. И. Киреев и др., Биохимия, 71, 6 (2006).
- Z. Zhou, R. Yan, W. Jiang, and J. M. K. Irudayaraj, Nanoscale Adv., 3 (4), 1019 (2021).
- M. Tark-Dame, R. van Driel, and D. W. Heermann, J. Cell Sci., 124 (6), 839 (2011).
- K. Maeshima, S. Tamura, J. C. Hansen, and Y. Itoh, Curr. Opin. Cell Biol., 64, 77 (2020).
- M. Egli, Chem. Biol., 9, 277 (2002).
- A. A. Kornyshev, D. J. Lee, S. Leikin, and A. Wynveen, Rev. Mod. Phys., 79, 943 (2007).
- A. G. Cherstvy, Phys. Chem. Chem. Phys., 13, 9942 (2011).
- Z. J. Tan and S. J. Chen, Biophys. J., 91 (2), 518 (2006).
- V. A. Bloomfield, Biopolymers, 44 (3), 269 (1997).
- P. M. Schwarz, A. Felthauser, T. M. Fletcher, and J. C. Hansen, Biochemistry, 35 (13), 4009-(1996).
- M. de Frutos, E. Raspaud, A. Leforestier, and F. Livolant, Biophys. J., 81 (2), 1127 (2001).
- C. A. Davey, and T. J. Richmond, Proc. Natl. Acad. Sci. USA, 99 (17), 11169 (2002).
- A. Bertin, S. Mangenot, M. Renouard, et al., Biophys J., 93, 3652 (2007).
- N. Korolev, A. Allahverdi, Ye. Yang, et al., Biophys. J., 99, 1896 (2010).
- A. Zinchenko, N. V. Berezhnoy, S. Wang, et al., Nucl. Acids Res., 46, 635 (2018).
- M. Krafcikova, S. Dzatko, C. Caron, et al., J. Am. Chem. Soc., 141 (34), 13281 (2019).
- J. Ellenberg, A. Walter, C. Chapuis, and S. Huetol, J. Struct. Biol., 184 (3), 445 (2013).
- P. J. Giannasca, R. A. Horowitz, and C. L. Woodcock, J. Cell Sci., 105 (2), 551 (1993).
- T. Ohyama, Int. J. Mol. Sci., 20 (17), 4232 (2019).
- M. A. Billett and T. J. Hall, Nucl. Acids Res., 6 (8), 2929 (1979).
- Y. Shimamoto, S. Tamura, H. Masumoto, and K. Maeshima, Mol. Biol. Cell, 28 (11), 1580 (2017).
- S. Schnell and R. Hancock, Methods Mol. Biol., 463, 3 (2008).
- R. Hancock, Biochemistry (Mosc.), 83 (4), 326 (2018).
- R. Strick, P. L. Strissel, K. Gavrilov, and R. Levi-Setti, J. Cell Biol., 155 (6), 899 (2001).
- N. Korolev, O. V. Vorontsova, and L. Nordenskiold, Prog. Biophys. Mol. Biol., 95, 23 (2007).
- S. E. Farr, E. J. Woods, J. A. Joseph, et al., Nat. Commun., 12 (1), 2883 (2021).
- А. Н. Прусов, Т. А. Смирнова и Г. Я. Коломийцева, Биохимия, 80 (3), 427 (2015).
- А. С. Спирин, Биохимия, 23, 656 (1976).
- A. Prado, C. Puyo, J. Arlucea, et al., J. Colloid Interface Sci., 177 (1), 9 (1996).
- N. A. Touchette and R. D. Cole, Proc. Natl. Acad. Sci. USA, 82, 2642 (1985).
- C. Balbi, M. L. Abelmoschi, L. Gogioso, S. Parodi, et al., Biochemistry, 28, 3220 (1989).
- C. Nicolini, A. Diaspro, L. Vergani, and G. Cittadini, Int. J. Biol. Macromol., 10, 137 (1988).
- M. Almagor and R. D. Cole, Biochemistry, 28, 5688 (1989).
- N. A. Touchette and R. D. Cole, Biochemistry, 31, 1842 (1992).
- A. N. Prusov, G. Ya. Kolomijtseva, and T. A. Smirnova, Pharmaceut. Biol., 55, 687 (2017).
- B. Cavazza, G. Brizzolara, G. Lazzarini, et al., Biochemistry, 30 (37), 9060 (1991).
- C. Balbi, P. Sanna, P. Barboro, et al., Biophys. J., 77 (5), 2725, (1999).
- S. Noriega, G. Budhiraja, and A. Subramanian, Int. J. Biochem. Cell Biol., 44 (8), 1331 (2012).
- M. Almagor and R. D. Cole, J. Biol. Chem., 264, 6515 (1989).
- А. Н. Прусов, Т. А. Смирнова и Г. Я. Коломийцева, Биохимия, 83 (10), 1534 (2018).
- Z. Darzynkiewicz, F. Traganos, T. Sharpless, and M. R. Melamed, J. Cell Biol., 68 (1), 1(1976).
- X. Ni and R. D. Cole, Biochemistry, 33 (31), 9276 (1994).
- I. Sissoeff, J. Grisvard, and E. Guill6, Prog. Biophys. Mol. Biol., 31 (2), 165 (1976).
- Y. P. Blagoi, V. A. Sorokin, V. A. Valeyev, et al., Biopolymers, 17 (5), 1103 (1978).
- А. П. Власов, Л. И. Яхонтова и В. Т.Андрианов, Биофизика, 36 (3), 437(1991).
- K. Serec, S. D. Babic, R. Podgornik and S. Tomic, Nucl. Acids Res., 44, 178456 (2016).
- I. Koltover, K. Wagner, and C. R. Safinya, Proc. Natl. Acad. Sci. USA, 97 (26), 14046 (2000).
- A. A. Kornyshev and S. Leikin, J. Chem. Phys., 107, 3656 (1997).
- A. G. Cherstvy and A. A. Kornyshev, J. Phys. Chem., 109 (26), 13024 (2005).
- A. G. Cherstvy and V. B. Teif, J. Biol. Phys., 39 (3), 363 (2013).
- Zh.-L. Zhang, Y. Y. Wu, K. Xi, et al., Biophys. J., 113, 517 (2017).
- G. R. Clark, C. J. Squire, L. J. Baker, et al., Nucl. Acids Res., 28 (5), 1259 (2000).
- L. McFail-Isom, X. Shui, and L. Williams, Biochemistry, 37 (49), 17105 (1998).
- J. E. Morgan, J. W. Blankenship, and H. R. Matthews, Arch. Biochem. Biophys., 246 (1), 225 (1986).
- G. S. Ott, R. Ziegler, and W. R. Bauer, Biochemistry, 14 (15), 3431 (1975).
- J. G. Duguid, V. A. Bloomfield, J. M. Benevides, and G. J. Thomas, Jr., Biophys. J., 69 (6), 2623 (1995).
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