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 language | English |
|---|---|
| Pages (from-to) | 332-338 |
| Number of pages | 7 |
| Journal | Nature Chemical Biology |
| Volume | 11 |
| Issue number | 5 |
| DOIs | |
| Publication status | Published - 2015 May 1 |
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ASJC Scopus subject areas
- Molecular Biology
- Cell Biology
Cite this
Monitoring methionine sulfoxide with stereospecific mechanism-based fluorescent sensors. / Tarrago, Lionel; Péterfi, Zalán; Lee, Byung Cheon; Michel, Thomas; Gladyshev, Vadim N.
In: Nature Chemical Biology, Vol. 11, No. 5, 01.05.2015, p. 332-338.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Monitoring methionine sulfoxide with stereospecific mechanism-based fluorescent sensors
AU - Tarrago, Lionel
AU - Péterfi, Zalán
AU - Lee, Byung Cheon
AU - Michel, Thomas
AU - Gladyshev, Vadim N.
PY - 2015/5/1
Y1 - 2015/5/1
N2 - 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.
AB - 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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UR - http://www.scopus.com/inward/citedby.url?scp=84940005486&partnerID=8YFLogxK
U2 - 10.1038/nchembio.1787
DO - 10.1038/nchembio.1787
M3 - Article
C2 - 25799144
AN - SCOPUS:84940005486
VL - 11
SP - 332
EP - 338
JO - Nature Chemical Biology
JF - Nature Chemical Biology
SN - 1552-4450
IS - 5
ER -