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

Submitted: 25 February 2014
Accepted: 17 March 2014
Published: 2 May 2014
Abstract Views: 2094
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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 γ-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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Supporting Agencies

Grant Agency of Czech Republic (Grant Nr., P302/10/1022, P302/12/G157, and 13-07822S). EU-COST Action TD0905, EU Marie Curie PIRSES-GA-2010-269156-LCS.
J. Suchánková, Academy of Sciences of the Czech Republic
Institute of Biophysics, Department of Cytology and Cytometry
S. Legartová, Academy of Sciences of the Czech Republic
Institute of Biophysics, Department of Cytology and Cytometry.
P. Sehnalová, Academy of Sciences of the Czech Republic
Institute of Biophysics, Department of Cytology and Cytometry
S. Kozubek, Academy of Sciences of the Czech Republic
Institute of Biophysics, Department of Cytology and Cytometry
S. Valente, Instituto Pasteur - Fondazione Cenci Bolognetti, University of Rome La Sapienza
Department of Chemistry and Drug Technology
D. Labella, Instituto Pasteur - Fondazione Cenci Bolognetti, University of Rome La Sapienza
Department of Chemistry and Drug Technology
A. Mai, Instituto Pasteur - Fondazione Cenci Bolognetti, University of Rome La Sapienza
Department of Chemistry and Drug Technology
C. Eckerich, Foundation for Research and Technology Hellas
Institute of Molecular Biology and Biotechnology, Department of Biomedical Research (IMBB-FORTH)
F.O. Fackelmayer, Foundation for Research and Technology Hellas
Institute of Molecular Biology and Biotechnology, Department of Biomedical Research (IMBB-FORTH)
D.V. Sorokin, Masaryk University
Faculty of Informatics, Centre for Biomedical Image Analysis
E. Bartova, Academy of Sciences of the Czech Republic
Institute of Biophysics, Department of Cytology and Cytometry

How to Cite

Suchánková, J., Legartová, S., Sehnalová, P., Kozubek, S., Valente, S., Labella, D., Mai, A., Eckerich, C., Fackelmayer, F., Sorokin, D., & Bartova, E. (2014). PRMT1 arginine methyltransferase accumulates in cytoplasmic bodies that respond to selective inhibition and DNA damage. European Journal of Histochemistry, 58(2). https://doi.org/10.4081/ejh.2014.2389