Cargando…

PRMT1 Arginine Methyltransferase Accumulates in Cytoplasmic Bodies that Respond to Selective Inhibition and DNA Damage

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, splicin...

Descripción completa

Detalles Bibliográficos
Autores principales: Suchánková, J., Legartová, S., Sehnalová, P., Kozubek, S., Valente, S., Labella, D., Mai, A., Eckerich, C., Fackelmayer, F.O., Sorokin, D.V., Bártová, E.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: PAGEPress Publications, Pavia, Italy 2014
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4083328/
https://www.ncbi.nlm.nih.gov/pubmed/24998928
http://dx.doi.org/10.4081/ejh.2014.2389
_version_ 1782324363245125632
author Suchánková, J.
Legartová, S.
Sehnalová, P.
Kozubek, S.
Valente, S.
Labella, D.
Mai, A.
Eckerich, C.
Fackelmayer, F.O.
Sorokin, D.V.
Bártová, E.
author_facet Suchánková, J.
Legartová, S.
Sehnalová, P.
Kozubek, S.
Valente, S.
Labella, D.
Mai, A.
Eckerich, C.
Fackelmayer, F.O.
Sorokin, D.V.
Bártová, E.
author_sort Suchánková, J.
collection PubMed
description 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 their, size was reduced, and they 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 over-expression. 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.
format Online
Article
Text
id pubmed-4083328
institution National Center for Biotechnology Information
language English
publishDate 2014
publisher PAGEPress Publications, Pavia, Italy
record_format MEDLINE/PubMed
spelling pubmed-40833282014-07-07 PRMT1 Arginine Methyltransferase Accumulates in Cytoplasmic Bodies that Respond to Selective Inhibition and DNA Damage Suchánková, J. Legartová, S. Sehnalová, P. Kozubek, S. Valente, S. Labella, D. Mai, A. Eckerich, C. Fackelmayer, F.O. Sorokin, D.V. Bártová, E. Eur J Histochem Original Paper 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 their, size was reduced, and they 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 over-expression. 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. PAGEPress Publications, Pavia, Italy 2014-05-02 /pmc/articles/PMC4083328/ /pubmed/24998928 http://dx.doi.org/10.4081/ejh.2014.2389 Text en ©Copyright J. Suchánková et al. http://creativecommons.org/licenses/by-nc/3.0/ This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/3.0/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Original Paper
Suchánková, J.
Legartová, S.
Sehnalová, P.
Kozubek, S.
Valente, S.
Labella, D.
Mai, A.
Eckerich, C.
Fackelmayer, F.O.
Sorokin, D.V.
Bártová, E.
PRMT1 Arginine Methyltransferase Accumulates in Cytoplasmic Bodies that Respond to Selective Inhibition and DNA Damage
title PRMT1 Arginine Methyltransferase Accumulates in Cytoplasmic Bodies that Respond to Selective Inhibition and DNA Damage
title_full PRMT1 Arginine Methyltransferase Accumulates in Cytoplasmic Bodies that Respond to Selective Inhibition and DNA Damage
title_fullStr PRMT1 Arginine Methyltransferase Accumulates in Cytoplasmic Bodies that Respond to Selective Inhibition and DNA Damage
title_full_unstemmed PRMT1 Arginine Methyltransferase Accumulates in Cytoplasmic Bodies that Respond to Selective Inhibition and DNA Damage
title_short PRMT1 Arginine Methyltransferase Accumulates in Cytoplasmic Bodies that Respond to Selective Inhibition and DNA Damage
title_sort prmt1 arginine methyltransferase accumulates in cytoplasmic bodies that respond to selective inhibition and dna damage
topic Original Paper
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4083328/
https://www.ncbi.nlm.nih.gov/pubmed/24998928
http://dx.doi.org/10.4081/ejh.2014.2389
work_keys_str_mv AT suchankovaj prmt1argininemethyltransferaseaccumulatesincytoplasmicbodiesthatrespondtoselectiveinhibitionanddnadamage
AT legartovas prmt1argininemethyltransferaseaccumulatesincytoplasmicbodiesthatrespondtoselectiveinhibitionanddnadamage
AT sehnalovap prmt1argininemethyltransferaseaccumulatesincytoplasmicbodiesthatrespondtoselectiveinhibitionanddnadamage
AT kozubeks prmt1argininemethyltransferaseaccumulatesincytoplasmicbodiesthatrespondtoselectiveinhibitionanddnadamage
AT valentes prmt1argininemethyltransferaseaccumulatesincytoplasmicbodiesthatrespondtoselectiveinhibitionanddnadamage
AT labellad prmt1argininemethyltransferaseaccumulatesincytoplasmicbodiesthatrespondtoselectiveinhibitionanddnadamage
AT maia prmt1argininemethyltransferaseaccumulatesincytoplasmicbodiesthatrespondtoselectiveinhibitionanddnadamage
AT eckerichc prmt1argininemethyltransferaseaccumulatesincytoplasmicbodiesthatrespondtoselectiveinhibitionanddnadamage
AT fackelmayerfo prmt1argininemethyltransferaseaccumulatesincytoplasmicbodiesthatrespondtoselectiveinhibitionanddnadamage
AT sorokindv prmt1argininemethyltransferaseaccumulatesincytoplasmicbodiesthatrespondtoselectiveinhibitionanddnadamage
AT bartovae prmt1argininemethyltransferaseaccumulatesincytoplasmicbodiesthatrespondtoselectiveinhibitionanddnadamage