Multicolor monitoring of the proteasomes catalytic signature

Melanie A. Priestman, Qunzhao Wang, Finith E. Jernigan, Ruma Chowdhury, Marion Schmidt, David S. Lawrence

Research output: Contribution to journalArticle

4 Scopus citations

Abstract

The proteasome, a validated anticancer target, participates in an array of biochemical activities, which range from the proteolysis of defective proteins to antigen presentation. We report the preparation of biochemically and photophysically distinct green, red, and far-red real-time sensors designed to simultaneously monitor the proteasomes chymotrypsin-, trypsin-, and caspase-like activities, respectively. These sensors were employed to assess the effect of simultaneous multiple active site catalysis on the kinetic properties of the individual subunits. Furthermore, we have found that the catalytic signature of the proteasome varies depending on the source, cell type, and disease state. Trypsin-like activity is more pronounced in yeast than in mammals, whereas chymotrypsin-like activity is the only activity detectable in B-cells (unlike other mammalian cells). Furthermore, chymotrypsin-like activity is more prominent in transformed B cells relative to their counterparts from healthy donors.

Original languageEnglish (US)
Pages (from-to)433-440
Number of pages8
JournalACS Chemical Biology
Volume10
Issue number2
DOIs
StatePublished - Feb 20 2015

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Medicine

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    Priestman, M. A., Wang, Q., Jernigan, F. E., Chowdhury, R., Schmidt, M., & Lawrence, D. S. (2015). Multicolor monitoring of the proteasomes catalytic signature. ACS Chemical Biology, 10(2), 433-440. https://doi.org/10.1021/cb5007322