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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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    Authors
    Osborne, Tanesha C.
    Obianyo, Obiamaka
    Zhang, Xing
    Cheng, Xiaodong
    Thompson, Paul R
    UMass Chan Affiliations
    Department of Biochemistry and Molecular Pharmacology
    Document Type
    Journal Article
    Publication Date
    2007-11-20
    Keywords
    Amino Acid Sequence
    Animals
    Binding Sites
    Catalysis
    Enzyme Inhibitors
    Histones
    Humans
    Kinetics
    Mass Spectrometry
    Methylation
    Models, Molecular
    Molecular Sequence Data
    Peptides
    Protein-Arginine N-Methyltransferases
    inhibitors
    Rats
    Recombinant Proteins
    Repressor Proteins
    Substrate Specificity
    Biochemistry
    Enzymes and Coenzymes
    Medicinal-Pharmaceutical Chemistry
    Therapeutics
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    Link to Full Text
    http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2723811/
    Abstract
    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.
    Source
    Biochemistry. 2007 Nov 20;46(46):13370-81. Link to article on publisher's site. Epub 2007 Oct 26.
    DOI
    10.1021/bi701558t
    Permanent Link to this Item
    http://hdl.handle.net/20.500.14038/50067
    Notes

    At the time of publication, Paul Thompson was not yet affiliated with UMass Medical School.

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    Link to Article in PubMed
    ae974a485f413a2113503eed53cd6c53
    10.1021/bi701558t
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