Monitoring methionine sulfoxide with stereospecific mechanism-based fluorescent sensors

Lionel Tarrago, Zalán Péterfi, Byung Cheon Lee, Thomas Michel, Vadim N. Gladyshev

Research output: Contribution to journalArticle

31 Citations (Scopus)

Abstract

Methionine can be reversibly oxidized to methionine sulfoxide (MetO) under physiological and pathophysiological conditions, but its use as a redox marker suffers from the lack of tools to detect and quantify MetO within cells. In this work, we created a pair of complementary stereospecific genetically encoded mechanism-based ratiometric fluorescent sensors of MetO by inserting a circularly permuted yellow fluorescent protein between yeast methionine sulfoxide reductases and thioredoxins. The two sensors, respectively named MetSOx and MetROx for their ability to detect S and R forms of MetO, were used for targeted analysis of protein oxidation, regulation and repair as well as for monitoring MetO in bacterial and mammalian cells, analyzing compartment-specific changes in MetO and examining responses to physiological stimuli.

Original languageEnglish
Pages (from-to)332-338
Number of pages7
JournalNature Chemical Biology
Volume11
Issue number5
DOIs
Publication statusPublished - 2015 May 1

ASJC Scopus subject areas

  • Molecular Biology
  • Cell Biology

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