The DOI matches its Crossref record; 57 of the 57 references it cites were found in a registry or an index.
The Novel Human Protein Arginine N-Methyltransferase PRMT6 Is a Nuclear Enzyme Displaying Unique Substrate Specificity
Open accessAbstract
Protein arginine methylation is a prevalent posttranslational modification in eukaryotic cells that has been implicated in signal transduction, the metabolism of nascent pre-RNA, and the transcriptional activation processes. In searching the human genome for protein arginine N-methyltransferase (PRMT) family members, a novel gene has been found on chromosome 1 that encodes for an apparent methyltransferase, PRMT6. The polypeptide chain of PRMT6 is 41.9 kDa consisting of a catalytic core sequence common to other PRMT enzymes. Expressed as a glutathione S-transferase fusion protein, PRMT6 demonstrates type I PRMT activity, capable of forming both omega-N(G)-monomethylarginine and asymmetric omega-N(G),N(G)-dimethylarginine derivatives on the recombinant glycine- and arginine-rich substrate in a processive manner with a specific activity of 144 pmol methyl groups transferred min(-1) mg(-1) enzyme. A comparison of substrate specificity reveals that PRMT6 is functionally distinct from two previously characterized type I enzymes, PRMT1 and PRMT4. In addition, PRMT6 displays automethylation activity; it is the first PRMT to do so. This novel human PRMT, which resides solely in the nucleus when fused to the green fluorescent protein, joins a family of enzymes with diverse functions within cells.
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Cites
Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4
LAEMMLI, U. K. (1970) · Nature · doi:10.1038/227680a0 · Cited by 249,961
Gapped BLAST and PSI-BLAST: a new generation of protein database search programs
Altschul, S. (1997) · Nucleic Acids Research · doi:10.1093/nar/25.17.3389 · Cited by 73,302
Initial sequencing and analysis of the human genome
International Human Genome Sequencing Consortium, Whitehead Institute for Biomedical Research, C. F. G. R., Lander, E. S., Linton, L. M., Birren, B., Nusbaum, C., Zody, M. C., Baldwin, J., Devon, K., Dewar, K., et al. (2001) · Nature · doi:10.1038/35057062 · Cited by 24,216
The sequence of the human genome
Venter, J. C., Adams, M. D., Myers, E. W., Li, P. W., Mural, R. J., Sutton, G. G., Smith, H. O., Yandell, M., Evans, C. A., Holt, R. A., et al. (2001) · Science · doi:10.1126/science.1058040 · Cited by 13,909
Current Protocols in Molecular Biology
Teplitz, R. (1989) · JAMA: The Journal of the American Medical Association · doi:10.1001/jama.1989.03420090114049 · Cited by 1,803
Techniques in Protein Chemistry
(1993) · Journal of the American Society for Mass Spectrometry · doi:10.1016/1044-0305(93)80012-n · Cited by 1,298
Regulation of Transcription by a Protein Methyltransferase
Chen, D., Ma, H., Hong, H., Koh, S. S., Huang, S.-M., Schurter, B. T., Aswad, D. W., & Stallcup, M. R. (1999) · Science · doi:10.1126/science.284.5423.2174 · Cited by 1,211
Measuring conformational dynamics of biomolecules by single molecule fluorescence spectroscopy.
Weiss, S. (2000) · Nature Structural Biology · doi:10.1038/78941 · Cited by 723
Techniques in protein chemistry
Pataki, G. (1967) · Journal of Chromatography A · doi:10.1016/s0021-9673(01)86077-5 · Cited by 660
RNA and Protein Interactions Modulated by Protein Arginine Methylation
Gary, J. D., & Clarke, S. (1998) · Progress in Nucleic Acid Research and Molecular Biology · doi:10.1016/s0079-6603(08)60825-9 · Cited by 500
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Protein arginine methyltransferases and cancer
Yang, Y., & Bedford, M. T. (2013) · Nature Reviews Cancer · doi:10.1038/nrc3409 · Cited by 1,083
Self-citationPal, S., Vishwanath, S. N., Erdjument-Bromage, H., Tempst, P., & Sif, S. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.21.9630-9645.2004 · Cited by 592
Role of Protein Methylation in Regulation of Transcription
Lee, D. Y., Teyssier, C., Strahl, B. D., & Stallcup, M. R. (2005) · Endocrine Reviews · doi:10.1210/er.2004-0008 · Cited by 455
Chemical mechanisms of histone lysine and arginine modifications
Smith, B. C., & Denu, J. M. (2009) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2008.06.005 · Cited by 390
Epigenetic tools (The Writers, The Readers and The Erasers) and their implications in cancer therapy
Biswas, S., & Rao, C. M. (2018) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2018.08.021 · Cited by 389
Metadata
- Authors
- Frankel, A., Yadav, N., Lee, J., Branscombe, T. L., Clarke, S., & Bedford, M. T.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2002-02
- Volume
- 277
- Issue
- 5
- Pages
- 3537-3543
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2166612636
- Cited by
- 334
- References
- 57
- FWCI
- 6.48
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- Frankel, A., Yadav, N., Lee, J., Branscombe, T. L., Clarke, S., & Bedford, M. T. (2002). The Novel Human Protein Arginine N-Methyltransferase PRMT6 Is a Nuclear Enzyme Displaying Unique Substrate Specificity. Journal of Biological Chemistry. https://doi.org/10.1074/jbc.m108786200
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