The GATA transcription factor ELT-2 modulates both the expression and methyltransferase activity of PRMT-1 in Caenorhabditis elegans. (18th January 2018)
- Record Type:
- Journal Article
- Title:
- The GATA transcription factor ELT-2 modulates both the expression and methyltransferase activity of PRMT-1 in Caenorhabditis elegans. (18th January 2018)
- Main Title:
- The GATA transcription factor ELT-2 modulates both the expression and methyltransferase activity of PRMT-1 in Caenorhabditis elegans
- Authors:
- Araoi, Sho
Daitoku, Hiroaki
Yokoyama, Atsuko
Kako, Koichiro
Hirota, Keiko
Fukamizu, Akiyoshi - Abstract:
- Abstract: Protein arginine methyltransferase 1 (PRMT1) catalyzes asymmetric arginine dimethylation of cellular proteins and thus modulates various biological processes, including gene regulation, RNA metabolism, cell signaling and DNA repair. Since prmt-1 null mutant completely abolishes asymmetric dimethylarginine in C. elegans, PRMT-1 is thought to play a crucial role in determining levels of asymmetric arginine dimethylation. However, the mechanism underlying the regulation of PRMT-1 activity remains largely unknown. Here, we explored for transcription factors that induce the expression of PRMT-1 by an RNAi screen using transgenic C. elegans harbouring prmt-1 promoter upstream of gfp . Of 529 clones, we identify a GATA transcription factor elt-2 as a positive regulator of Pprmt-1:: gfp expression and show that elt-2 RNAi decreases endogenous PRMT-1 expression at mRNA and protein levels. Nevertheless, surprisingly arginine methylation levels are increased when elt-2 is silenced, implying that erythroid-like transcription factor (ELT)-2 may also have ability to inhibit methyltransferase activity of PRMT-1. Supporting this idea, GST pull-down and co-immunoprecipitation assays demonstrate the interaction between ELT-2 and PRMT-1. Furthermore, we find that ELT-2 interferes with PRMT-1-induced arginine methylation in a dose-dependent manner. Collectively, our results illustrate the two modes of PRMT-1 regulation, which could determine the levels of asymmetric arginineAbstract: Protein arginine methyltransferase 1 (PRMT1) catalyzes asymmetric arginine dimethylation of cellular proteins and thus modulates various biological processes, including gene regulation, RNA metabolism, cell signaling and DNA repair. Since prmt-1 null mutant completely abolishes asymmetric dimethylarginine in C. elegans, PRMT-1 is thought to play a crucial role in determining levels of asymmetric arginine dimethylation. However, the mechanism underlying the regulation of PRMT-1 activity remains largely unknown. Here, we explored for transcription factors that induce the expression of PRMT-1 by an RNAi screen using transgenic C. elegans harbouring prmt-1 promoter upstream of gfp . Of 529 clones, we identify a GATA transcription factor elt-2 as a positive regulator of Pprmt-1:: gfp expression and show that elt-2 RNAi decreases endogenous PRMT-1 expression at mRNA and protein levels. Nevertheless, surprisingly arginine methylation levels are increased when elt-2 is silenced, implying that erythroid-like transcription factor (ELT)-2 may also have ability to inhibit methyltransferase activity of PRMT-1. Supporting this idea, GST pull-down and co-immunoprecipitation assays demonstrate the interaction between ELT-2 and PRMT-1. Furthermore, we find that ELT-2 interferes with PRMT-1-induced arginine methylation in a dose-dependent manner. Collectively, our results illustrate the two modes of PRMT-1 regulation, which could determine the levels of asymmetric arginine dimethylation in C. elegans . … (more)
- Is Part Of:
- Journal of biochemistry. Volume 163:Number 5(2018:May)
- Journal:
- Journal of biochemistry
- Issue:
- Volume 163:Number 5(2018:May)
- Issue Display:
- Volume 163, Issue 5 (2018)
- Year:
- 2018
- Volume:
- 163
- Issue:
- 5
- Issue Sort Value:
- 2018-0163-0005-0000
- Page Start:
- 433
- Page End:
- 440
- Publication Date:
- 2018-01-18
- Subjects:
- C. elegans -- enzyme -- gene -- inhibitors -- methyltransferase -- organisms -- PRMT-1 -- protein -- ELT-2 -- transcription factor -- expression
Biochemistry -- Periodicals
Biochemistry -- Periodicals
Electronic journals
572.05 - Journal URLs:
- http://wwwsoc.nii.ac.jp/jbiochem/jb/index.htm ↗
http://jb.oupjournals.org/ ↗
http://jb.oxfordjournals.org/ ↗
http://www.bcasj.or.jp/jbindex.html ↗
http://ukcatalogue.oup.com/ ↗ - DOI:
- 10.1093/jb/mvy012 ↗
- Languages:
- English
- ISSNs:
- 0021-924X
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 4952.000000
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