A glutamate/aspartate switch controls product specificity in a protein arginine methyltransferase
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- Erik W. Debler
- Laboratory of Cell Biology, The Rockefeller University, New York, NY 10065;
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- Kanishk Jain
- Department of Chemistry and Biochemistry and The Molecular Biology Institute, University of California, Los Angeles, CA 90095;
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- Rebeccah A. Warmack
- Department of Chemistry and Biochemistry and The Molecular Biology Institute, University of California, Los Angeles, CA 90095;
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- You Feng
- Department of Chemistry and Biochemistry and The Molecular Biology Institute, University of California, Los Angeles, CA 90095;
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- Steven G. Clarke
- Department of Chemistry and Biochemistry and The Molecular Biology Institute, University of California, Los Angeles, CA 90095;
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- Günter Blobel
- Laboratory of Cell Biology, The Rockefeller University, New York, NY 10065;
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- Pete Stavropoulos
- Laboratory of Cell Biology, The Rockefeller University, New York, NY 10065;
書誌事項
- 公開日
- 2016-02-08
- 権利情報
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- http://www.pnas.org/preview_site/misc/userlicense.xhtml
- DOI
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- 10.1073/pnas.1525783113
- 公開者
- Proceedings of the National Academy of Sciences
この論文をさがす
説明
<jats:title>Significance</jats:title> <jats:p> Posttranslational modifications in proteins profoundly modulate their function, and enzymes that generate these modifications therefore have key regulatory roles in a wide array of biological processes. Protein arginine methyltransferases (PRMTs) attach methyl group(s) to arginines and differ in their product specificity, as they form either monomethyl arginine (MMA), asymmetric dimethylarginine (ADMA), or symmetric dimethylarginine (SDMA), each of which relays specific biological signals. Although the members of the PRMT family are structurally highly homologous, the precise molecular basis of their product specificity has not been determined. Based on our structure of <jats:italic>Tb</jats:italic> PRMT7, which explicitly forms MMA, we identified a glutamate residue as a key determinant of its product specificity, and we were able to engineer a <jats:italic>Tb</jats:italic> PRMT7 mutant capable of ADMA formation. </jats:p>
収録刊行物
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- Proceedings of the National Academy of Sciences
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Proceedings of the National Academy of Sciences 113 (8), 2068-2073, 2016-02-08
Proceedings of the National Academy of Sciences
