The DOI matches its Crossref record; 26 of the 26 references it cites were found in a registry or an index.
PRMT1 Is the Predominant Type I Protein Arginine Methyltransferase in Mammalian Cells
Open accessAbstract
Type I protein arginine methyltransferases catalyze the formation of asymmetric omega-N(G),N(G)-dimethylarginine residues by transferring methyl groups from S-adenosyl-L-methionine to guanidino groups of arginine residues in a variety of eucaryotic proteins. The predominant type I enzyme activity is found in mammalian cells as a high molecular weight complex (300-400 kDa). In a previous study, this protein arginine methyltransferase activity was identified as an additional activity of 10-formyltetrahydrofolate dehydrogenase (FDH) protein. However, immunodepletion of FDH activity in RAT1 cells and in murine tissue extracts with antibody to FDH does not diminish type I methyltransferase activity toward the methyl-accepting substrates glutathione S-transferase fibrillarin glycine arginine domain fusion protein or heterogeneous nuclear ribonucleoprotein A1. Similarly, immunodepletion with anti-FDH antibody does not remove the endogenous methylating activity for hypomethylated proteins present in extracts from adenosine dialdehyde-treated RAT1 cells. In contrast, anti-PRMT1 antibody can remove PRMT1 activity from RAT1 extracts, murine tissue extracts, and purified rat liver FDH preparations. Tissue extracts from FDH(+/+), FDH(+/-), and FDH(-/-) mice have similar protein arginine methyltransferase activities but high, intermediate, and undetectable FDH activities, respectively. Recombinant glutathione S-transferase-PRMT1, but not purified FDH, can be cross-linked to the methyl-donor substrate S-adenosyl-L-methionine. We conclude that PRMT1 contributes the major type I protein arginine methyltransferase enzyme activity present in mammalian cells and tissues.
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Cites
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Cited by
Nott, T. J., Petsalaki, E., Farber, P., Jervis, D., Fussner, E., Plochowietz, A., Craggs, T. D., Bazett-Jones, D. P., Pawson, T., Forman-Kay, J. D., et al. (2015) · Molecular Cell · doi:10.1016/j.molcel.2015.01.013 · Cited by 1,803
Protein arginine methyltransferases and cancer
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Roles and regulation of histone methylation in animal development
Jambhekar, A., Dhall, A., & Shi, Y. (2019) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-019-0151-1 · Cited by 556
A Transcriptional Switch Mediated by Cofactor Methylation
Xu, W., Chen, H., Du, K., Asahara, H., Tini, M., Emerson, B. M., Montminy, M., & Evans, R. M. (2001) · Science · doi:10.1126/science.1065961 · Cited by 416
Friesen, W. J., Paushkin, S., Wyce, A., Massenet, S., Pesiridis, G. S., Van Duyne, G., Rappsilber, J., Mann, M., & Dreyfuss, G. (2001) · Molecular and Cellular Biology · doi:10.1128/mcb.21.24.8289-8300.2001 · Cited by 408
Metadata
- Authors
- Tang, J., Frankel, A., Cook, R. J., Kim, S., Paik, W. K., Williams, K. R., Clarke, S., & Herschman, H. R.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2000-03
- Volume
- 275
- Issue
- 11
- Pages
- 7723-7730
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2156211472
- Cited by
- 489
- References
- 26
- FWCI
- 3.49
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- Tang, J., Frankel, A., Cook, R. J., Kim, S., Paik, W. K., Williams, K. R., Clarke, S., & Herschman, H. R. (2000). PRMT1 Is the Predominant Type I Protein Arginine Methyltransferase in Mammalian Cells. Journal of Biological Chemistry. https://doi.org/10.1074/jbc.275.11.7723
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