Доклады Академии наукДоклады Академии наук0869-5652The Russian Academy of Sciences1860310.31857/S0869-56524893318-320Research ArticleHistone tails promote PARP1-dependent structural rearrangements in nucleosomesMaluchenkoN. V.mal_nat@mail.ruSultanovD. S.mal_nat@mail.ruKotovaE. Yu.mal_nat@mail.ruKirpichnikovM. P.<p>Academician of the Russian Academy of Sciences</p>mal_nat@mail.ruStuditskyV. M.mal_nat@mail.ruFeofanovA. V.mal_nat@mail.ruLomonosov Moscow State UniversityFox Chase Cancer CenterShemyakin & Ovchinnikov Institute of Bioorganic Chemistry of the Russian Academy of Sciences2911201948933183200912201909122019Copyright © 2019, Russian academy of sciences2019<p class="a"><span lang="EN-US">PARP1 alters the wrapping of nucleosomal DNA on the surface of the histone octamer, thereby modulating the accessibility of different genome sites to nuclear protein factors. Here we show that non-structured histone tails participate in the PARP1-induced structural rearrangements in nucleosomes, facilitate and stabilize them, but do not affect the enzymatic activity of PARP1.</span></p>histone tailsPARP1nucleosomespFRETN концы гистоновPARP1нуклеосомаspFRET[Wang Y., LuoW., Wang Y. // DNA Repair (Amsterdam). 2019. V. 8. P. 102651.][Posavec Marjanović M., Crawford K., Ahel I. // Semin. Cell Dev Biol. 2017. V. 63. P. 102-113.][Thomas C., Ji.Y., Wu C., Datz H., Boyle C., Mac-Leod B., Patel S., Ampofo M., Currie M., Harbin J., Pechenkina K., Lodhi N., Johnson S.J., Tulin A.V. // Proc. Natl Acad. Sci. USA. 2019. V. 116. P. 9941-9946.][Krishnakumar R., Gamble M., Frizzell K.M., Berrocal J.G., Kininis M., Kraus W.L. // Science. 2008. V. 319. P. 819-821.][Liu Z., Kraus K. // Mol. Cell. 2017. V. 65. P. 589-603.][Sultanov D.C., Gerasimova N.S., Kudrjashova K., Maluchenko N.V., Kotova E.Y., Langelier M.F., Pascal J.M., Kirpichnikov M.P., Feofanov A.V., Studitsky V.M. // AIMS Genet. 2017. V. 4. P. 21-31.][Azad G.K., Swagatika K.M., Kumawat R., Tomar R.S. // J. Mol. Biol. 2018. V. 430. Р. 3051-3067.][Gaykalova D.A., Kulaeva O.I., Bondarenko V.A., Studitsky V.M. // Methods Mol. Biol. 2009. V. 523. P. 109-123.][Luger K., Rechsteiner T., Flaus A.J., Waye M.M., Richmond T.J. // J. Mol. Biol. 1997. V. 27. P. 301-311.][Langelier M.F., Planck J.L., Servent K.M., Pascal J.M. // Methods Mol. Biol. 2011. 780. P. 209-226.][Clark N.J., Kramer M., Muthurajan U.M., Luger K. // J. Biol. Chem. 2012. V. 287. P. 32 430-32 439.][Kudryashova K.S., Nikitin D.V., Chertkov O.V., Gerasimova N.S., Valeva M.E., Studitsky V.M., Feofanov A.V. // Moscow Univ. Biol. Sciences Bulletin. 2015. V. 70. P. 189-193.]