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Protein Arginine Methyltransferase 1:  Positively Charged Residues in Substrate Peptides Distal to the Site of Methylation Are Important for Substrate Binding and Catalysis

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Department of Chemistry & Biochemistry, University of South Carolina, 631 Sumter Street, Columbia, South Carolina 29208, and Department of Biochemistry, Emory University School of Medicine, 1510 Clifton Road, Atlanta, Georgia 30322
Cite this: Biochemistry 2007, 46, 46, 13370–13381
Publication Date (Web):October 26, 2007
Copyright © 2007 American Chemical Society

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    Abstract Image

    Protein arginine methyltransferases (PRMTs) are a group of eukaryotic enzymes that catalyze the methylation of Arg residues in a variety of proteins (e.g., histones H3 and H4), and their activities influence a wide range of cellular processes, including cell growth, RNA splicing, differentiation, and transcriptional regulation. Dysregulation of these enzymes has been linked to heart disease and cancer, suggesting this enzyme family as a novel therapeutic target. To aid the development of PRMT inhibitors, we characterized the substrate specificity of both the rat and human PRMT1 orthologues using histone based peptide substrates. N- and C-terminal truncations to identify a minimal peptide substrate indicate that long-range interactions between enzyme and substrate are important for high rates of substrate capture. The importance of these long-range interactions to substrate capture were confirmed by “mutagenesis” experiments on a minimal peptide substrate. Inhibition studies on S-adenosyl-homocysteine, thioadenosine, methylthioadenosine, homocysteine, and sinefungin suggest that potent and selective bisubstrate analogue inhibitor(s) for PRMT1 can be developed by linking a histone based peptide substrate to homocysteine or sinefungin. Additionally, we present evidence that PRMT1 utilizes a partially processive mechanism to dimethylate its substrates.

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     This work was supported in part by the start up funds from the University of South Carolina Research Foundation (P.R.T.) and from a new investigator grant from the American Heart Association. T.C.O. is supported by an NSF GK-12 fellowship, O.O. is supported by an NIH-PREP fellowship (GM066526), and X.Z. and X.C. are supported by an NIH grant (GM068680).

     University of South Carolina.


     These authors contributed equally to this work.

     Emory University School of Medicine.


     To whom correspondence should be addressed:  Department of Chemistry & Biochemistry, University of South Carolina, 631 Sumter Street, Columbia, SC 29208. Tel:  (803)-777-6414. Fax:  (803)-777-9521. E-mail:  [email protected].

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    Please note: If you switch to a different device, you may be asked to login again with only your ACS ID.

    Your Mendeley pairing has expired. Please reconnect