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Activity-based protein profiling of protein arginine methyltransferase 1

Academic Article
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Overview

authors

  • Obianyo, O.
  • Causey, C. P.
  • Jones, J. E.
  • Thompson, Paul

publication date

  • October 2011

journal

  • ACS Chemical Biology  Journal

abstract

  • The protein arginine methyltransferases (PRMTs) are SAM-dependent enzymes that catalyze the mono- and dimethylation of peptidyl arginine residues. PRMT1 is the founding member of the PRMT family, and this isozyme is responsible for methylating ∼85% of the arginine residues in mammalian cells. Additionally, PRMT1 activity is aberrantly upregulated in heart disease and cancer. As a part of a program to develop isozyme-specific PRMT inhibitors, we recently described the design and synthesis of C21, a chloroacetamidine bearing histone H4 tail analogue that acts as an irreversible PRMT1 inhibitor. Given the covalent nature of the interaction, we set out to develop activity-based probes (ABPs) that could be used to characterize the physiological roles of PRMT1. Herein, we report the design, synthesis, and characterization of fluorescein-conjugated C21 (F-C21) and biotin-conjugated C21 (B-C21) as PRMT1-specific ABPs. Additionally, we provide the first evidence that PRMT1 activity is negatively regulated in a spatial and temporal fashion.

subject areas

  • Breast Neoplasms
  • Cell Line, Tumor
  • Drug Design
  • Enzyme Inhibitors
  • Female
  • Humans
  • Inhibitory Concentration 50
  • Protein-Arginine N-Methyltransferases
  • Repressor Proteins
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Identity

PubMed Central ID

  • PMC3199286

International Standard Serial Number (ISSN)

  • 1554-8929

Digital Object Identifier (DOI)

  • 10.1021/cb2001473

PubMed ID

  • 21838253
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Additional Document Info

start page

  • 1127

end page

  • 1135

volume

  • 6

issue

  • 10

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