Monitoring of Protein Arginine Deiminase Activity by Using Fluorescence Quenching: Multicolor Visualization of Citrullination

Authors

  • Prof. Qunzhao Wang,

    1. Department of Chemistry, Division of Chemical Biology and Medicinal Chemistry, and the Department of Pharmacology, University of North Carolina, Chapel Hill, NC 27599 (USA)
    Search for more papers by this author
  • Prof. Melanie A. Priestman,

    1. Department of Chemistry, Division of Chemical Biology and Medicinal Chemistry, and the Department of Pharmacology, University of North Carolina, Chapel Hill, NC 27599 (USA)
    Search for more papers by this author
  • Prof. David S. Lawrence

    Corresponding author
    1. Department of Chemistry, Division of Chemical Biology and Medicinal Chemistry, and the Department of Pharmacology, University of North Carolina, Chapel Hill, NC 27599 (USA)
    • Department of Chemistry, Division of Chemical Biology and Medicinal Chemistry, and the Department of Pharmacology, University of North Carolina, Chapel Hill, NC 27599 (USA)===

    Search for more papers by this author

  • We thank the NIH (CA159189) for financial support.

Abstract

original image

Colorful: The protein arginine deiminases are members of the enzyme family that catalyze posttranslational histone modification and consequent changes in gene expression. A visual readout of catalytic activity was developed that yields large fluorescence changes across the visible spectrum. The use of different fluorophores (see picture) enables the simultaneous multicolor monitoring of a mixture of histone-modifying enzymes.

Ancillary