Genetically encoded sensors of protein hydrodynamics and molecular proximity
Abstract
Significance The lumazine binding protein (LUMP) emits a cyan-colored fluorescence and has the longest average fluorescence lifetime of any genetically encoded fluorescent protein complex. Coupled with a small mass of 20 kDa, LUMP and its fusion with capture sequences are exploited as unique sensors of protein hydrodynamics and are shown to enable quantitative fluorescence anisotropy imaging of specific target proteins in vitro and in vivo. Moreover, the surface location of the lumazine probe is shown to improve the efficiency of Förster resonance energy transfer (FRET) with the Venus acceptor protein compared with CFP, which is used in the development of a new class of FRET-based sensor.
- Authors:
-
- Department of Bioengineering, University of California, Berkeley, CA 94720,, Lawrence Berkeley National Laboratory, Berkeley, CA 94720,
- Department of Bioengineering, University of California, Berkeley, CA 94720,
- Department of Physics, King’s College London, London WC2R 2LS, United Kingdom, and
- Department of Bioengineering, Santa Clara University, Santa Clara, CA 95053
- Publication Date:
- Sponsoring Org.:
- USDOE
- OSTI Identifier:
- 1235180
- Grant/Contract Number:
- LDRD
- Resource Type:
- Published Article
- Journal Name:
- Proceedings of the National Academy of Sciences of the United States of America
- Additional Journal Information:
- Journal Name: Proceedings of the National Academy of Sciences of the United States of America Journal Volume: 112 Journal Issue: 20; Journal ID: ISSN 0027-8424
- Publisher:
- Proceedings of the National Academy of Sciences
- Country of Publication:
- United States
- Language:
- English
Citation Formats
Hoepker, Alexander C., Wang, Ariel, Le Marois, Alix, Suhling, Klaus, Yan, Yuling, and Marriott, Gerard. Genetically encoded sensors of protein hydrodynamics and molecular proximity. United States: N. p., 2015.
Web. doi:10.1073/pnas.1424021112.
Hoepker, Alexander C., Wang, Ariel, Le Marois, Alix, Suhling, Klaus, Yan, Yuling, & Marriott, Gerard. Genetically encoded sensors of protein hydrodynamics and molecular proximity. United States. https://doi.org/10.1073/pnas.1424021112
Hoepker, Alexander C., Wang, Ariel, Le Marois, Alix, Suhling, Klaus, Yan, Yuling, and Marriott, Gerard. Thu .
"Genetically encoded sensors of protein hydrodynamics and molecular proximity". United States. https://doi.org/10.1073/pnas.1424021112.
@article{osti_1235180,
title = {Genetically encoded sensors of protein hydrodynamics and molecular proximity},
author = {Hoepker, Alexander C. and Wang, Ariel and Le Marois, Alix and Suhling, Klaus and Yan, Yuling and Marriott, Gerard},
abstractNote = {Significance The lumazine binding protein (LUMP) emits a cyan-colored fluorescence and has the longest average fluorescence lifetime of any genetically encoded fluorescent protein complex. Coupled with a small mass of 20 kDa, LUMP and its fusion with capture sequences are exploited as unique sensors of protein hydrodynamics and are shown to enable quantitative fluorescence anisotropy imaging of specific target proteins in vitro and in vivo. Moreover, the surface location of the lumazine probe is shown to improve the efficiency of Förster resonance energy transfer (FRET) with the Venus acceptor protein compared with CFP, which is used in the development of a new class of FRET-based sensor.},
doi = {10.1073/pnas.1424021112},
journal = {Proceedings of the National Academy of Sciences of the United States of America},
number = 20,
volume = 112,
place = {United States},
year = {Thu Apr 30 00:00:00 EDT 2015},
month = {Thu Apr 30 00:00:00 EDT 2015}
}
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https://doi.org/10.1073/pnas.1424021112
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