Informace o publikaci

PRMT1 arginine methyltransferase accumulates in cytoplasmic bodies that respond to selective inhibition and DNA damage

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SUCHÁNKOVÁ Jana LEGARTOVÁ Soňa SEHNALOVÁ Petra KOZUBEK Stanislav VALENTE Sergio LABELLA Donatella MAI Antonello ECKERICH Carmen FACKELMAYER Frank O. SOROKIN Dmitry BÁRTOVÁ Eva

Rok publikování 2014
Druh Článek v odborném periodiku
Časopis / Zdroj European Journal of Histochemistry
Fakulta / Pracoviště MU

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Citace
Doi http://dx.doi.org/10.4081/ejh.2014.2389
Obor Genetika a molekulární biologie
Klíčová slova Epigenetics; PRMTs; epi-drugs; arginine methylation; DNA repair
Popis Protein arginine methyltransferases (PRMTs) are responsible for symmetric and asymmetric methylation of arginine residues of nuclear and cytoplasmic proteins. In the nucleus, PRMTs belong to important chromatin modifying enzymes of immense functional significance that affect gene expression, splicing and DNA repair. By time-lapse microscopy we have studied the sub-cellular localization and kinetics of PRMT1 after inhibition of PRMT1 and after irradiation. Both transiently expressed and endogenous PRMT1 accumulated in cytoplasmic bodies that were located in the proximity of the cell nucleus. The shape and number of these bodies were stable in untreated cells. However, when cell nuclei were microirradiated by UV-A, the mobility of PRMT1 cytoplasmic bodies increased, size was reduced, and disappeared within approximately 20 min. The same response occurred after gamma-irradiation of the whole cell population, but with delayed kinetics. Treatment with PRMT1 inhibitors induced disintegration of these PRMT1 cytoplasmic bodies and prevented formation of 53BP1 nuclear bodies (NBs) that play a role during DNA damage repair. The formation of 53BP1 NBs was not influenced by PRMT1 overexpression. Taken together, we show that PRMT1 concentrates in cytoplasmic bodies, which respond to DNA injury in the cell nucleus, and to treatment with various PRMT1 inhibitors.
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