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A Genetically Encoded Fluorescent Reporter of Histone Phosphorylation in Living Cells
Author(s) -
Lin ChiWang,
Ting Alice Y.
Publication year - 2004
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.200353375
Subject(s) - förster resonance energy transfer , phosphorylation , histone , histone h3 , domain (mathematical analysis) , phosphoserine , fluorescence , serine , chemistry , energy transfer , microbiology and biotechnology , computational biology , biology , gene , biochemistry , physics , mathematical analysis , mathematics , quantum mechanics , molecular physics
An increase in FRET indicates phosphorylation of histone H3 at serine 28. The protein‐based reporter (see picture) responds to phosphorylation through intramolecular complexation between a substrate domain derived from histone H3 and a linked phosphoserine‐recognition domain. The reporter is also effective inside living mammalian cells. FRET=fluorescence resonance energy transfer.