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

J 2014

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

SUCHÁNKOVÁ, Jana, Soňa LEGARTOVÁ, Petra SEHNALOVÁ, Stanislav KOZUBEK, Sergio VALENTE et. al.

Basic information

Original name

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

Authors

SUCHÁNKOVÁ, Jana (203 Czech Republic), Soňa LEGARTOVÁ (703 Slovakia), Petra SEHNALOVÁ (203 Czech Republic), Stanislav KOZUBEK (203 Czech Republic), Sergio VALENTE (380 Italy), Donatella LABELLA (380 Italy), Antonello MAI (380 Italy), Carmen ECKERICH (300 Greece), Frank O. FACKELMAYER (300 Greece), Dmitry SOROKIN (643 Russian Federation, guarantor, belonging to the institution) and Eva BÁRTOVÁ (203 Czech Republic)

Edition

European Journal of Histochemistry, Pavia, Italy, PAGEPress, 2014, 1121-760X

Other information

Language

English

Type of outcome

Článek v odborném periodiku

Field of Study

10609 Biochemical research methods

Country of publisher

Italy

Confidentiality degree

není předmětem státního či obchodního tajemství

Impact factor

Impact factor: 2.042

RIV identification code

RIV/00216224:14330/14:00073586

Organization unit

Faculty of Informatics

DOI

http://dx.doi.org/10.4081/ejh.2014.2389

UT WoS

000338624700013

Keywords in English

Epigenetics; PRMTs; epi-drugs; arginine methylation; DNA repair

Abstract

V originále

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.

Links

CZ.1.07/2.3.00/30.0030, interní kód MU

Name: Rozvoj lidských zdrojů pro oblast buněčné biologie

Investor: Ministry of Education, Youth and Sports of the CR, 2.3 Human resources in research and development

GBP302/12/G157, research and development project

Name: Dynamika a organizace chromosomů během buněčného cyklu a při diferenciaci v normě a patologii

Investor: Czech Science Foundation

Citovat

SUCHÁNKOVÁ, Jana, Soňa LEGARTOVÁ, Petra SEHNALOVÁ, Stanislav KOZUBEK, Sergio VALENTE, Donatella LABELLA, Antonello MAI, Carmen ECKERICH, Frank O. FACKELMAYER, Dmitry SOROKIN and Eva BÁRTOVÁ. PRMT1 arginine methyltransferase accumulates in cytoplasmic bodies that respond to selective inhibition and DNA damage. European Journal of Histochemistry. Pavia, Italy: PAGEPress, 2014, vol. 58, No 2, p. 139-151. ISSN 1121-760X. Available from: https://dx.doi.org/10.4081/ejh.2014.2389.

@article{1179522,
   author = {Suchánková, Jana and Legartová, Soňa and Sehnalová, Petra and Kozubek, Stanislav and Valente, Sergio and Labella, Donatella and Mai, Antonello and Eckerich, Carmen and Fackelmayer, Frank O. and Sorokin, Dmitry and Bártová, Eva},
   article_location = {Pavia, Italy},
   article_number = {2},
   doi = {http://dx.doi.org/10.4081/ejh.2014.2389},
   keywords = {Epigenetics; PRMTs; epi-drugs; arginine methylation; DNA repair},
   language = {eng},
   issn = {1121-760X},
   journal = {European Journal of Histochemistry},
   title = {PRMT1 arginine methyltransferase accumulates in cytoplasmic bodies that respond to selective inhibition and DNA damage},
   volume = {58},
   year = {2014}
}

TY  - JOUR
ID  - 1179522
AU  - Suchánková, Jana - Legartová, Soňa - Sehnalová, Petra - Kozubek, Stanislav - Valente, Sergio - Labella, Donatella - Mai, Antonello - Eckerich, Carmen - Fackelmayer, Frank O. - Sorokin, Dmitry - Bártová, Eva
PY  - 2014
TI  - PRMT1 arginine methyltransferase accumulates in cytoplasmic bodies that respond to selective inhibition and DNA damage
JF  - European Journal of Histochemistry
VL  - 58
IS  - 2
SP  - 139-151
EP  - 139-151
PB  - PAGEPress
SN  - 1121760X
KW  - Epigenetics
KW  - PRMTs
KW  - epi-drugs
KW  - arginine methylation
KW  - DNA repair
N2  - 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.
ER  -

SUCHÁNKOVÁ, Jana, Soňa LEGARTOVÁ, Petra SEHNALOVÁ, Stanislav KOZUBEK, Sergio VALENTE, Donatella LABELLA, Antonello MAI, Carmen ECKERICH, Frank O. FACKELMAYER, Dmitry SOROKIN and Eva BÁRTOVÁ. PRMT1 arginine methyltransferase accumulates in cytoplasmic bodies that respond to selective inhibition and DNA damage. \textit{European Journal of Histochemistry}. Pavia, Italy: PAGEPress, 2014, vol.~58, No~2, p.~139-151. ISSN~1121-760X. Available from: https://dx.doi.org/10.4081/ejh.2014.2389.

Detailed Information on Publication Record