Structural tuning of the fluorescent protein iLOV for improved photostability

Christie, J.M. , Hitomi, K., Arvai, A.S., Hartfield, K.A., Mettlen, M., Pratt, A.J., Tainer, J.A. and Getzoff, E.D. (2012) Structural tuning of the fluorescent protein iLOV for improved photostability. Journal of Biological Chemistry, 287(26), pp. 22295-22304. (doi:10.1074/jbc.M111.318881)

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Abstract

Background: iLOV is a fluorescent flavoprotein engineered from the plant blue light receptor phototropin. <p/>Results: Structures reveal altered protein-chromophore interactions within the flavin-binding cavity of iLOV when compared with its progenitors. Directed evolution further anchored the chromophore to increase iLOV photostability by an order of magnitude. <p/>Conclusion: Improving iLOV photostability by constraining its fluorophore establishes a framework for fine-tuning fluorescence. <p/>Significance: Enhanced photostability increases iLOV utility as an oxygen-independent fluorescent reporter.

Item Type:Articles
Status:Published
Refereed:Yes
Glasgow Author(s) Enlighten ID:Christie, Professor John
Authors: Christie, J.M., Hitomi, K., Arvai, A.S., Hartfield, K.A., Mettlen, M., Pratt, A.J., Tainer, J.A., and Getzoff, E.D.
College/School:College of Medical Veterinary and Life Sciences > Institute of Molecular Cell and Systems Biology
Journal Name:Journal of Biological Chemistry
Publisher:American Society for Biochemistry and Molecular Biology, Inc.
ISSN:0021-9258
Published Online:09 May 2012

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