PABP1 identified as an arginine methyltransferase substrate using high‐density protein arrays
- 1 March 2002
- journal article
- Published by Springer Nature in EMBO Reports
- Vol. 3 (3) , 268-273
- https://doi.org/10.1093/embo-reports/kvf052
Abstract
The arginine methyltransferases CARM1 and PRMT1 associate with the p160 family of nuclear hormone receptor coactivators. This association enhances transcriptional activation by nuclear receptors. We describe a method for identifying arginine N‐methyltransferase substrates using arrayed high‐density protein membranes to perform solid‐phase supported enzyme reactions in the presence of the methyl donor S‐adenosyl‐L‐methionine. Using this screen, we identified distinct substrates for CARM1 and PRMT1. All PRMT1 substrates harbor the expected GGRGG methylation motif, whereas the peptide sequence comparisons of the CARM1 substrates revealed no such motif. The predominant CARM1 substrate identified in this screen was PABP1. We mapped the methylated region of this RNA binding molecule in vitro and demonstrate that PABP1 is indeed methylated in vivo. Prior to these findings, the only known substrate for CARM1 was histone H3. We broaden the number of CARM1 targets and suggest a role for CARM1 in regulating transcription/translation.Keywords
This publication has 24 references indexed in Scilit:
- Methylation of Histone H4 at Arginine 3 Facilitating Transcriptional Activation by Nuclear Hormone ReceptorScience, 2001
- State of the ArgCell, 2001
- SMN, the Product of the Spinal Muscular Atrophy Gene, Binds Preferentially to Dimethylarginine-Containing Protein TargetsMolecular Cell, 2001
- Delivering messages from the 3′ endProceedings of the National Academy of Sciences, 2001
- Methylation of Histone H3 by Coactivator-Associated Arginine Methyltransferase 1Biochemistry, 2001
- X-ray structure of the human hyperplastic discs protein: An ortholog of the C-terminal domain of poly(A)-binding proteinProceedings of the National Academy of Sciences, 2001
- TARPP, a novel protein that accompanies TCR gene rearrangement and thymocyte educationEuropean Journal of Immunology, 2001
- Synergistic Enhancement of Nuclear Receptor Function by p160 Coactivators and Two Coactivators with Protein Methyltransferase ActivitiesPublished by Elsevier ,2001
- Arginine Methylation Inhibits the Binding of Proline-rich Ligands to Src Homology 3, but Not WW, DomainsJournal of Biological Chemistry, 2000
- Regulation of Transcription by a Protein MethyltransferaseScience, 1999