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

Result code in IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14330%2F14%3A00073586" target="_blank" >RIV/00216224:14330/14:00073586 - isvavai.cz</a>

Result on the web

<a href="http://dx.doi.org/10.4081/ejh.2014.2389" target="_blank" >http://dx.doi.org/10.4081/ejh.2014.2389</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.4081/ejh.2014.2389" target="_blank" >10.4081/ejh.2014.2389</a>

Result language

angličtina

Original language name

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

Original language 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 PRMT1accumulated 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.

Czech name

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Czech description

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Type

J_x - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)

CEP classification

EB - Genetics and molecular biology

OECD FORD branch

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Project

<a href="/en/project/GBP302%2F12%2FG157" target="_blank" >GBP302/12/G157: Dynamics and Organization of Chromosomes in the Cell Cycle and during Differentiation under Normal and Pathological Conditions</a><br>

Continuities

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Publication year

2014

Confidentiality

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Name of the periodical

European Journal of Histochemistry

ISSN

1121-760X

e-ISSN

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Volume of the periodical

58

Issue of the periodical within the volume

2

Country of publishing house

IT - ITALY

Number of pages

13

Pages from-to

139-151

UT code for WoS article

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EID of the result in the Scopus database

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