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

被引:117
|
作者
Cook, JR
Lee, JH
Yang, ZH
Krause, CD
Herth, N
Hoffmann, R
Pestka, S
机构
[1] Univ Med & Dent New Jersey, Robert Wood Johnson Med Sch, Piscataway, NJ 08854 USA
[2] Univ Leipzig, Ctr Biotechnol & Biomed, Fac Chem & Mineral, D-04103 Leipzig, Germany
[3] PBL Biomed Labs, Piscataway, NJ 08854 USA
[4] Canc Inst New Jersey, New Brunswick, NJ 08903 USA
关键词
PRMT; protein arginine methyltransferase; type II; symmetric dimethylarginine; immunolocalization; structure modeling; methylation; FBXO11; FLJ12673; F-box; zinc finger; beta-propeller;
D O I
10.1016/j.bbrc.2006.01.167
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
We have identified a protein, FLJ12673 or FBXO 11, 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. (c) 2006 Elsevier Inc. All rights reserved.
引用
收藏
页码:472 / 481
页数:10
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