Monitoring methionine sulfoxide with stereospecific mechanism-based fluorescent sensors
- Authors
- Tarrago, Lionel; Peterfi, Zalan; Lee, Byung Cheon; Michel, Thomas; Gladyshev, Vadim N.
- Issue Date
- 5월-2015
- Publisher
- NATURE PUBLISHING GROUP
- Citation
- NATURE CHEMICAL BIOLOGY, v.11, no.5, pp.332 - U123
- Indexed
- SCIE
SCOPUS
- Journal Title
- NATURE CHEMICAL BIOLOGY
- Volume
- 11
- Number
- 5
- Start Page
- 332
- End Page
- U123
- URI
- https://scholar.korea.ac.kr/handle/2021.sw.korea/93682
- DOI
- 10.1038/NCHEMBIO.1787
- ISSN
- 1552-4450
- 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.
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Collections - Graduate School > Department of Biotechnology > 1. Journal Articles
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