Extraction of histone H1 and decondensation of nuclear chromatin with various Mg-dependent organization levels under treatment with polyglutamic acid and distamycin

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• 作者：A. N. Prusov ; T. A. Smirnova ; G. Ya. Kolomijtseva
• 关键词：cell nuclei ; chromatin ; levels of structural organization ; distamycin ; polyglutamic acid ; histone H1 ; CD spectra
• 刊名：Biochemistry (Moscow)
• 出版年：2015
• 出版时间：March 2015
• 年：2015
• 卷：80
• 期：3
• 页码：356-365
• 全文大小：815 KB
• 参考文献：1. Polyakov, V Yu, Zatsepina, O V, Kireev, I I, Prusov, A N, Fais, D, Sheval, Ye V, Koblyakova, Yu V, Golyshev, S A, Chentsov, Yu S (2006) Structural and functional model of mitotic chromosome. Biochemistry (Moscow) 71: pp. 1-9 <a class="external" href="http://dx.doi.org/10.1134/S0006297906010019" target="_blank" title="It opens in new window">CrossRefa>
  2. Maeshima, K, Imai, R, Tamura, S, Nozaki, T (2014) Chromatin as dynamic 10-nm fibers. Chromosoma 123: pp. 225-237 <a class="external" href="http://dx.doi.org/10.1007/s00412-014-0460-2" target="_blank" title="It opens in new window">CrossRefa>
  3. Hansen, J C (2012) Human mitotic chromosome structure: what happened to the 30-nm fiber. EMBO J. 31: pp. 1621-1623 <a class="external" href="http://dx.doi.org/10.1038/emboj.2012.66" target="_blank" title="It opens in new window">CrossRefa>
  4. Grigoryev, S A, Woodcock, C L (2012) Chromatin organization -the 30 nm fiber. Exp. Cell Res. 318: pp. 1448-1455 <a class="external" href="http://dx.doi.org/10.1016/j.yexcr.2012.02.014" target="_blank" title="It opens in new window">CrossRefa>
  5. Simpson, R T, Thoma, F, Brubaker, J M (2006) Chromatin reconstituted from tandemly repeated cloned DNA fragments and core histones: a model system for study of higher order structure. Cell 42: pp. 799-808 <a class="external" href="http://dx.doi.org/10.1016/0092-8674(85)90276-4" target="_blank" title="It opens in new window">CrossRefa>
  6. Ilatovsky, A V, Lebedev, D V, Filatov, M V, Petukhov, M G, Isaev-Ivanov, V V (2012) Current picture of structural organization of chromatin. Tsitologiya 54: pp. 298-305
  7. Yevdokimov, Yu M, Salyanov, V I, Skuridin, S G (2007) Liquid crystal DNA forms. Part I. Condensed condition of DNA in vivo and in vitro. Tekhnol. Zhivykh Sistem 4: pp. 3-30
  8. Schnell, S, Hancock, R (2008) The intranuclear environment. Methods Mol. Biol. 463: pp. 3-19 <a class="external" href="http://dx.doi.org/10.1007/978-1-59745-406-3_1" target="_blank" title="It opens in new window">CrossRefa>
  9. Th’ng, J P, Sung, R Ye M, Hendzel, M J (2005) H1 family histones in the nucleus. Control of binding and localization by the C-terminal domain. J. Biol. Chem. 280: pp. 27809-27814 <a class="external" href="http://dx.doi.org/10.1074/jbc.M501627200" target="_blank" title="It opens in new window">CrossRefa>
  10. Harshman, W, Young, N L, Parthun, M R, Freitas, M A (2013) H1 histones: current perspectives and challenges. Nucleic Acids Res. 41: pp. 9593-9609 <a class="external" href="http://dx.doi.org/10.1093/nar/gkt700" target="_blank" title="It opens in new window">CrossRefa>
  11. Luger, K, Hansen, J C (2005) Nucleosome and chromatin fiber dynamics. Curr. Opin. Struct. Biol. 15: pp. 188-196 <a class="external" href="http://dx.doi.org/10.1016/j.sbi.2005.03.006" target="_blank" title="It opens in new window">CrossRefa>
  12. Maeshima, K, Hihara, S, Eltsov, M (2010) Chromatin structure: does the 30-nm fiber exist in vivo?. Curr. Opin. Cell Biol. 22: pp. 291-297 <a class="external" href="http://dx.doi.org/10.1016/j.ceb.2010.03.001" target="_blank" title="It opens in new window">CrossRefa>
  13. Kiryanov, G I, Manamshjan, T A, Polyakov, V Yu, Fais, D, Chentsov, Yu S (1976) Levels of granular organization of chromatin fibers. FEBS Lett. 67: pp. 323-327 <a class="external" href="http://dx.doi.org/10.1016/0014-5793(76)80557-1" target="_blank" title="It opens in new window">CrossRefa>
  14. Prusov, A N, Smirnova, T A, Kolomijtseva, G Ya (2013) Effect of chromatin structure, antibiotics and endogenous methylation of histones on phosphorylation of H1 and H3 histones under protein kinase A conditions in rat liver nuclei in vitro. Biochemistry (Moscow) 78: pp. 176-184 <a class="external" href="http://dx.doi.org/10.1134/S0006297913020065" target="_blank" title="It opens in new window">CrossRefa>
  15. Prusov, A N, Smirnova, T A, Kolomijtseva, G Ya (2010) Effect of dystamycin, chromomycin, and UV light on extraction of polyglutamic acid of histone H1 from rat liver nuclei. Biochemistry (Moscow) 75: pp. 1331-1341 <a class="external" href="http://dx.doi.org/10.1134/S0006297910110040" target="_blank" title="It opens in new window">CrossRefa>
  16. Spirin, A S (1958) Spectrophotometric determination of total nucleic acids. Biokhimiya 23: pp. 656-661
  17. Laemmli, U K (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227: pp. 680-685 <a class="external" href="http://dx.doi.org/10.1038/227680a0" target="_blank" title="It opens in new window">CrossRefa>
  18. Olins, D E, Olins, A L (1972) Physical studies of isolated eucaryotic nuclei. J. Cell Biol. 58: pp. 715-736 <a class="external" href="http://dx.doi.org/10.1083/jcb.53.3.715" target="_blank" title="It opens in new window">CrossRefa>
  19. Wagner, T, Spelsberg, T C (1971) Aspects of chromosomal structure. I. Circular dichroism studies. Biochemistry 10: pp. 2599
• 刊物类别：Biomedical and Life Sciences
• 刊物主题：Life Sciences
  Biochemistry
  Bioorganic Chemistry
  Microbiology
  Biomedicine
  Russian Library of Science
  
• 出版者：MAIK Nauka/Interperiodica distributed exclusively by Springer Science+Business Media LLC.
• ISSN：1608-3040

文摘

Chromatin in rat liver nuclei under conditions of low ionic strength (20-5 mM) and [Mg2+] from 2 to 5 mM has a condensed structure (100-00 nm globules) and gives the same CD signal (320-40 nm) at interaction with the antibiotic distamycin A (DM). Reducing [Mg2+] to 1 mM leads to chromatin decondensation to 30 nm structures and increases the CD signal. Poly-L-glutamic acid (PG) at weight ratio PG/DNA = 6 and in the presence of 5 mM Mg2+ extracts only about 1/8 of nuclear histone H1, preserving a condensed chromatin structure. Removal of about 1/4 of H1 at 3 mM Mg2+ leads to chromatin decondensation to 30 nm fibrils. Extraction of about half of histone H1 at [Mg2+] ?2 mM results in chromatin refolding to nucleosome fibrils. PG-decondensation leads to a significant increase in the CD signal. The main H1 extraction occurs in 1- min, but at all Mg2+ concentrations the more slowly PG extracted fraction is found comprising 5-% of nuclear H1. About 25% of leaving nuclear H1 can be extracted by PG in the presence of saturating DM concentration (molar DM/DNA = 0.1). H1 release depends significantly on the PG concentration. However, even at high weight ratio PG/DNA = 30 and DM/DNA = 0.1, about 5-0% of histone H1 remained in the nuclei. Decondensation of chromatin in the nucleus is not always proportional to the yield of extracted histone H1 and is weakened in the presence of positively charged DM or high concentrations of PG. Our results show that the interaction of DM with chromatin depends primarily on chromatin packaging, while PG extraction depends on [Mg2+] supporting this packaging.