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A genetically encoded fluorescent reporter of ATP:ADP ratio
Open accessAbstract
We constructed a fluorescent sensor of adenylate nucleotides by combining a circularly permuted variant of GFP with a bacterial regulatory protein, GlnK1, from Methanococcus jannaschii. The sensor's affinity for Mg-ATP was <100 nM, as seen for other members of the bacterial PII regulator family, a surprisingly high affinity given that normal intracellular ATP concentration is in the millimolar range. ADP bound the same site of the sensor as Mg-ATP, competing with it, but produced a smaller change in fluorescence. At physiological ATP and ADP concentrations, the binding site is saturated, but competition between the two substrates causes the sensor to behave as a nearly ideal reporter of the ATP:ADP concentration ratio. This principle for sensing the ratio of two analytes by competition at a high-affinity site probably underlies the normal functioning of PII regulatory proteins. The engineered sensor, Perceval, can be used to monitor the ATP:ADP ratio during live-cell imaging.
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Metadata
- Authors
- Berg, J., Hung, Y. P., & Yellen, G.
- Venue
- Nature Methods
- Published
- 2009-01-04
- Volume
- 6
- Issue
- 2
- Pages
- 161-166
- ISSN
- 1548-7091 (ISSN-L)
- 1548-7105
- OpenAlex
- W2129558617
- Cited by
- 475
- References
- 1
- FWCI
- 12.75
- Type
- journal article
- Language
- en
- Open access
- green
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