FBXO11/PRMT9, a new protein arginine methyltransferase, symmetrically dimethylates arginine residues

We have identified a protein, FLJ12673 or FBXO11, that contains domains characteristically present in protein arginine methyltransferases (PRMTs). Immuno-purified protein expressed from one of the four splice variants in HeLa cells and in Escherichia coli exhibited methyltransferase activity. Monome...

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Bibliographic Details
Published in:Biochemical and biophysical research communications 2006-04, Vol.342 (2), p.472-481
Main Authors: Cook, Jeffry R., Lee, Jin-Hyung, Yang, Zhi-Hong, Krause, Christopher D., Herth, Nicole, Hoffmann, Ralf, Pestka, Sidney
Format: Article
Language:English
Subjects:
Amino Acid Motifs
Amino Acid Sequence
Animals
Arginine - metabolism
Base Sequence
Escherichia coli
Evolution, Molecular
F-box
F-Box Proteins - genetics
F-Box Proteins - metabolism
FBXO11
FLJ12673
HeLa Cells
Humans
Immunolocalization
Isoenzymes - genetics
Isoenzymes - metabolism
Methylation
Mice
Molecular Sequence Data
Multigene Family
PRMT
Protein arginine methyltransferase
Protein-Arginine N-Methyltransferases - genetics
Protein-Arginine N-Methyltransferases - metabolism
Rats
Sequence Alignment
Sequence Analysis, Protein
Structure modeling
Symmetric dimethylarginine
Type II
Zinc finger
β-propeller
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Summary:We have identified a protein, FLJ12673 or FBXO11, that contains domains characteristically present in protein arginine methyltransferases (PRMTs). Immuno-purified protein expressed from one of the four splice variants in HeLa cells and in Escherichia coli exhibited methyltransferase activity. Monomethylarginine, symmetric, and asymmetric dimethylarginine (SDMA, ADMA) were formed on arginine residues. Accordingly, we have designated the protein PRMT9. PRMT9 is the third member of the PRMT family that forms SDMA modifications in proteins. Structurally, this protein is distinct from all other known PRMTs implying that convergent evolution allowed this protein to develop the ability to methylate arginine residues and evolved elements conserved in PRMTs to accomplish this.
ISSN:0006-291X
1090-2104
DOI:10.1016/j.bbrc.2006.01.167