This work was supported by MIT start-up funds and by grants from the National Institutes of Health (K22-HG002671-01), the Office of Naval Research (N00014-03-1-0456), and the Camille and Henry Dreyfus New Faculty Award Program (NF-02-003). C.-W.L. was supported by a Merck/MIT predoctoral fellowship. The Multiuser Facility for the Study of Complex Macromolecular Systems (NSF-0070319) is also gratefully acknowledged. The Msk-1 expression plasmid was a gift from Prof. Jiahuai Han. We are grateful to Sean Liu and Dr. Brian J. Schneider for technical assistance, and to Profs. Jin Zhang and Michael B. Yaffe for helpful discussions.
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Communication
A Genetically Encoded Fluorescent Reporter of Histone Phosphorylation in Living Cells†
Article first published online: 19 MAY 2004
DOI: 10.1002/anie.200353375
Copyright © 2004 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim
Additional Information
How to Cite
Lin, C.-W. and Ting, A. Y. (2004), A Genetically Encoded Fluorescent Reporter of Histone Phosphorylation in Living Cells. Angew. Chem. Int. Ed., 43: 2940–2943. doi: 10.1002/anie.200353375
- †
Publication History
- Issue published online: 19 MAY 2004
- Article first published online: 19 MAY 2004
- Manuscript Revised: 19 MAR 2004
- Manuscript Received: 21 NOV 2003
Keywords:
- fluorescence;
- histones;
- imaging;
- phosphorylation;
- reporters
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.