Compliance with Ethical Standards
Funding: The support of Leiden University is kindly acknowledged.
Conflict of Interest: Matthijs van Haren declares that he has no conflict of interest. Nathaniel I.
Martin declares that he has no conflict of interest.
Ethical Approval: This article does not contain any studies with human participants or animals
performed by any of the authors.
References
1. Paik WK, Kim S (1967) Enzymatic methylation of protein fractions from calf thymus nuclei.
Biochem Biophys Res Commun 29:14–20
2. Paik WK, Kim S (1968) Protein methylase I. Purification and properties of the enzyme. J Biol
Chem 243:2108–2114
3. Boffa LC et al (1977) Distribution of NG, NG,-dimethylarginine in nuclear protein fractions.
Biochem Biophys Res Commun 74:969–976
4. Lee HW et al (1977) S-adenosylmethionine: protein-arginine methyltransferase. Purification
and mechanism of the enzyme. Biochemistry 16:78–85
5. Ghosh SK et al (1988) Purification and molecular identification of two protein methylases I
from calf brain. Myelin basic protein- and histone-specific enzyme. J Biol Chem
263:19024–19033
6. Najbauer J et al (1993) Peptides with sequences similar to glycine, arginine-rich motifs in
proteins interacting with RNA are efficiently recognized by methyltransferase(s) modifying
arginine in numerous proteins. J Biol Chem 268:10501–10509
7. Rajpurohit R et al (1994) Enzymatic methylation of recombinant heterogeneous nuclear RNP
protein A1. Dual substrate specificity for S-adenosylmethionine:histone-arginine
N-methyltransferase. J Biol Chem 269:1075–1082
8. Liu Q, Dreyfuss G (1995) In vivo and in vitro arginine methylation of RNA-binding proteins.
Mol Cell Biol 15:2800–2808
9. Lin WJ et al (1996) The mammalian immediate-early TIS21 protein and the leukemiaassociated BTG1 protein interact with a protein-arginine N-methyltransferase. J Biol Chem
271:15034–15044
10. Scott HS et al (1998) Identification and characterization of two putative human arginine
methyltransferases (HRMT1L1 and HRMT1L2). Genomics 48:330–340
Table 1 (continued)
PRMT
Type
Substrates
Function/disease relation
Effect by inhibition
PRMT8
Type I
GAR substrates
Histone H2A
Histone
4 Arg3
Tumour proteins
RNA-binding
proteins
PRMT8
(auto)
Essential for cell proliferation
Highly expressed in breast, head
and neck, glandular, cervical,
prostate and thyroid cancer
Involved in ALS
Knockdown halted cell proliferation and
caused cell death in fibroblasts and
glioblastoma cells
PRMT9
Type II
SAP145
Regulates splicing
Unknown
188
M. J. van Haren and N. I. Martin
Funding: The support of Leiden University is kindly acknowledged.
Conflict of Interest: Matthijs van Haren declares that he has no conflict of interest. Nathaniel I.
Martin declares that he has no conflict of interest.
Ethical Approval: This article does not contain any studies with human participants or animals
performed by any of the authors.
References
1. Paik WK, Kim S (1967) Enzymatic methylation of protein fractions from calf thymus nuclei.
Biochem Biophys Res Commun 29:14–20
2. Paik WK, Kim S (1968) Protein methylase I. Purification and properties of the enzyme. J Biol
Chem 243:2108–2114
3. Boffa LC et al (1977) Distribution of NG, NG,-dimethylarginine in nuclear protein fractions.
Biochem Biophys Res Commun 74:969–976
4. Lee HW et al (1977) S-adenosylmethionine: protein-arginine methyltransferase. Purification
and mechanism of the enzyme. Biochemistry 16:78–85
5. Ghosh SK et al (1988) Purification and molecular identification of two protein methylases I
from calf brain. Myelin basic protein- and histone-specific enzyme. J Biol Chem
263:19024–19033
6. Najbauer J et al (1993) Peptides with sequences similar to glycine, arginine-rich motifs in
proteins interacting with RNA are efficiently recognized by methyltransferase(s) modifying
arginine in numerous proteins. J Biol Chem 268:10501–10509
7. Rajpurohit R et al (1994) Enzymatic methylation of recombinant heterogeneous nuclear RNP
protein A1. Dual substrate specificity for S-adenosylmethionine:histone-arginine
N-methyltransferase. J Biol Chem 269:1075–1082
8. Liu Q, Dreyfuss G (1995) In vivo and in vitro arginine methylation of RNA-binding proteins.
Mol Cell Biol 15:2800–2808
9. Lin WJ et al (1996) The mammalian immediate-early TIS21 protein and the leukemiaassociated BTG1 protein interact with a protein-arginine N-methyltransferase. J Biol Chem
271:15034–15044
10. Scott HS et al (1998) Identification and characterization of two putative human arginine
methyltransferases (HRMT1L1 and HRMT1L2). Genomics 48:330–340
Table 1 (continued)
PRMT
Type
Substrates
Function/disease relation
Effect by inhibition
PRMT8
Type I
GAR substrates
Histone H2A
Histone
4 Arg3
Tumour proteins
RNA-binding
proteins
PRMT8
(auto)
Essential for cell proliferation
Highly expressed in breast, head
and neck, glandular, cervical,
prostate and thyroid cancer
Involved in ALS
Knockdown halted cell proliferation and
caused cell death in fibroblasts and
glioblastoma cells
PRMT9
Type II
SAP145
Regulates splicing
Unknown
188
M. J. van Haren and N. I. Martin