TY - JOUR
T1 - The novel human protein arginine N-methyltransferase PRMT6 is a nuclear enzyme displaying unique substrate specificity
AU - Frankel, Adam
AU - Yadav, Neelu
AU - Lee, Jaeho
AU - Branscombe, Tina L.
AU - Clarke, Steven
AU - Bedford, Mark T.
N1 - Funding Information:
★This work was supported by Science Foundation Ireland under Grant 05/IN/I886. We thank E. Hebrard for contributing the experiment shown in Figure 2.
PY - 2002/2/1
Y1 - 2002/2/1
N2 - 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 ω-NG-monomethylarginine and asymmetric ω-NG,NG-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.
AB - 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 ω-NG-monomethylarginine and asymmetric ω-NG,NG-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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U2 - 10.1074/jbc.M108786200
DO - 10.1074/jbc.M108786200
M3 - Article
C2 - 11724789
AN - SCOPUS:0036479327
SN - 0021-9258
VL - 277
SP - 3537
EP - 3543
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
IS - 5
ER -