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PRMT1 arginine methyltransferase accumulates in cytoplasmic bodies that respond to selective inhibition and DNA damage
- Source :
- European Journal of Histochemistry, Vol 58, Iss 2 (2014), European Journal of Histochemistry : EJH
- Publication Year :
- 2014
- Publisher :
- PAGEPress Publications, 2014.
-
Abstract
- 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.
- Subjects :
- Cytoplasm
Protein-Arginine N-Methyltransferases
Histology
Methyltransferase
Chromosomal Proteins, Non-Histone
Ultraviolet Rays
DNA repair
DNA damage
Biophysics
Biology
Mice
Gene expression
medicine
Animals
Humans
epi-drugs
lcsh:QH301-705.5
Original Paper
Intracellular Signaling Peptides and Proteins
Cell Biology
Molecular biology
arginine methylation
DNA-Binding Proteins
Repressor Proteins
Cell nucleus
medicine.anatomical_structure
lcsh:Biology (General)
Gamma Rays
Epigenetics
PRMTs
Tumor Suppressor p53-Binding Protein 1
Nucleus
DNA Damage
HeLa Cells
Subjects
Details
- ISSN :
- 20388306 and 1121760X
- Volume :
- 58
- Database :
- OpenAIRE
- Journal :
- European Journal of Histochemistry
- Accession number :
- edsair.doi.dedup.....3f55157fd18cda22c1315755d4188ad5