mCherry 与其他可见荧光蛋白之间荧光共振能量转移的Förster 距离。
Förster distances for fluorescence resonant energy transfer between mCherry and other visible fluorescent proteins.
机构信息
Department of Biochemistry and Physiology of Plants, Faculty of Biology, University of Bielefeld, D-33501 Bielefeld, Germany.
出版信息
Anal Biochem. 2010 Jul 1;402(1):105-6. doi: 10.1016/j.ab.2010.03.026. Epub 2010 Mar 27.
Abstract
We present, for the red fluorescent protein mCherry acting as both fluorescence resonant energy transfer (FRET) donor and acceptor, Förster critical distance (r(0)) values with five important visible fluorescent protein (VFP) variants as well as with itself. The pair EYFP-mCherry exhibits an r(0) of 5.66nm, equaling or exceeding any combination of VFPs reported previously. Moreover, mCherry should be an excellent chromophore for homo-FRET with an r(0) of 5.10nm for energy transfer between two mCherry moieties. Finally, mCherry exhibits higher r(0) values than does DsRed. These characteristics, combined with mCherry's rapid folding and excellent spectral properties, suggest that mCherry constitutes a valuable long-wavelength hetero-FRET acceptor and probe for homo-FRET experiments.
摘要
我们提出，对于既作为荧光共振能量转移（FRET）供体又作为受体的红色荧光蛋白 mCherry，与五个重要的可见荧光蛋白（VFP）变体以及自身相比，福斯特临界距离（r(0)）值。EYFP-mCherry 对显示出 5.66nm 的 r(0)，等于或超过以前报道的任何 VFP 组合。此外，mCherry 应该是同型 FRET 的极好发色团，两个 mCherry 部分之间的能量转移 r(0)为 5.10nm。最后，mCherry 的 r(0)值高于 DsRed。这些特性，加上 mCherry 快速折叠和出色的光谱特性，表明 mCherry 构成了一种有价值的长波长异 FRET 受体和同型 FRET 实验的探针。
相似文献
1
Förster distances for fluorescence resonant energy transfer between mCherry and other visible fluorescent proteins.mCherry 与其他可见荧光蛋白之间荧光共振能量转移的Förster 距离。
Anal Biochem. 2010 Jul 1;402(1):105-6. doi: 10.1016/j.ab.2010.03.026. Epub 2010 Mar 27.
2
Time-resolved FRET fluorescence spectroscopy of visible fluorescent protein pairs.可见荧光蛋白对的时间分辨荧光共振能量转移荧光光谱学
Eur Biophys J. 2010 Jan;39(2):241-53. doi: 10.1007/s00249-009-0528-8. Epub 2009 Aug 20.
3
Quantitative FRET analysis with the EGFP-mCherry fluorescent protein pair.使用EGFP-mCherry荧光蛋白对进行定量荧光共振能量转移分析。
Photochem Photobiol. 2009 Jan-Feb;85(1):287-97. doi: 10.1111/j.1751-1097.2008.00435.x. Epub 2008 Aug 27.
4
Self-assembled donor comprising quantum dots and fluorescent proteins for long-range fluorescence resonance energy transfer.用于长程荧光共振能量转移的由量子点和荧光蛋白组成的自组装供体。
J Am Chem Soc. 2008 Apr 9;130(14):4815-27. doi: 10.1021/ja078243f. Epub 2008 Mar 14.
5
Quantitative comparison of different fluorescent protein couples for fast FRET-FLIM acquisition.不同荧光蛋白偶联物用于快速 FRET-FLIM 获取的定量比较。
Biophys J. 2009 Oct 21;97(8):2368-76. doi: 10.1016/j.bpj.2009.07.044.
6
Sensitive detection of p65 homodimers using red-shifted and fluorescent protein-based FRET couples.使用红移和基于荧光蛋白的荧光共振能量转移对灵敏检测p65同二聚体。
PLoS One. 2007 Oct 10;2(10):e1011. doi: 10.1371/journal.pone.0001011.
7
Comparing the performance of mScarlet-I, mRuby3, and mCherry as FRET acceptors for mNeonGreen.比较 mScarlet-I、mRuby3 和 mCherry 作为 mNeonGreen 的 FRET 受体的性能。
PLoS One. 2020 Feb 5;15(2):e0219886. doi: 10.1371/journal.pone.0219886. eCollection 2020.
8
Modulation of Intracellular Quantum Dot to Fluorescent Protein Förster Resonance Energy Transfer via Customized Ligands and Spatial Control of Donor-Acceptor Assembly.通过定制配体和供体-受体组装的空间控制对细胞内量子点至荧光蛋白荧光共振能量转移的调控。
Sensors (Basel). 2015 Dec 4;15(12):30457-68. doi: 10.3390/s151229810.
9
Biosensor Optimization Using a Förster Resonance Energy Transfer Pair Based on mScarlet Red Fluorescent Protein and an mScarlet-Derived Green Fluorescent Protein.基于mScarlet红色荧光蛋白和mScarlet衍生绿色荧光蛋白的Förster共振能量转移对进行生物传感器优化
ACS Sens. 2023 Feb 24;8(2):587-597. doi: 10.1021/acssensors.2c01730. Epub 2023 Jan 24.
10
Characterization of a spectrally diverse set of fluorescent proteins as FRET acceptors for mTurquoise2.鉴定一组具有光谱多样性的荧光蛋白作为 mTurquoise2 的 FRET 供体。
Sci Rep. 2017 Sep 20;7(1):11999. doi: 10.1038/s41598-017-12212-x.
引用本文的文献
1
Detection of Protein Interactions and Dynamics During Viral Infection via Fluorescence Resonance Energy Transfer.通过荧光共振能量转移检测病毒感染过程中的蛋白质相互作用和动态变化
Methods Mol Biol. 2025;2940:387-398. doi: 10.1007/978-1-0716-4615-1_34.
2
Protein misfolding involving entanglements providesa structural explanation for the origin of stretched-exponential refolding kinetics.涉及缠结的蛋白质错误折叠为拉伸指数型重折叠动力学的起源提供了一种结构解释。
Sci Adv. 2025 Mar 14;11(11):eads7379. doi: 10.1126/sciadv.ads7379.
3
Dimerization of melanocortin 4 receptor controls puberty onset and body size polymorphism.黑皮质素 4 受体的二聚化控制着青春期的开始和体型多态性。
Front Endocrinol (Lausanne). 2023 Nov 10;14:1267590. doi: 10.3389/fendo.2023.1267590. eCollection 2023.
4
Interaction of human CRX and NRL in live HEK293T cells measured using fluorescence resonance energy transfer (FRET).应用荧光共振能量转移（FRET）技术在活的 HEK293T 细胞中检测人 CRX 和 NRL 的相互作用。
Sci Rep. 2022 Apr 28;12(1):6937. doi: 10.1038/s41598-022-10689-9.
5
Dynamic assembly of the mRNA m6A methyltransferase complex is regulated by METTL3 phase separation.mRNA m6A 甲基转移酶复合物的动态组装受 METTL3 相分离的调控。
PLoS Biol. 2022 Feb 10;20(2):e3001535. doi: 10.1371/journal.pbio.3001535. eCollection 2022 Feb.
6
Novel drug discovery platform for spinocerebellar ataxia, using fluorescence technology targeting β-III-spectrin.用于脊髓小脑共济失调的新型药物发现平台，使用针对β-III- spectrin 的荧光技术。
J Biol Chem. 2021 Jan-Jun;296:100215. doi: 10.1074/jbc.RA120.015417. Epub 2020 Dec 24.
7
A Novel FRET Approach Quantifies the Interaction Strength of Peroxisomal Targeting Signals and Their Receptor in Living Cells.一种新型 FRET 方法定量测定活细胞中过氧化物酶体靶向信号及其受体的相互作用强度。
Cells. 2020 Oct 30;9(11):2381. doi: 10.3390/cells9112381.
8
Morphological transformation enhances Tumor Retention by Regulating the Self-assembly of Doxorubicin-peptide Conjugates.形态转化通过调节阿霉素-肽缀合物的自组装增强肿瘤滞留。
Theranostics. 2020 Jul 9;10(18):8162-8178. doi: 10.7150/thno.45088. eCollection 2020.
9
Membrane Protein Dimerization in Cell-Derived Lipid Membranes Measured by FRET with MC Simulations.利用 MC 模拟的 FRET 技术测量细胞衍生的脂膜中的膜蛋白二聚体。
Biophys J. 2020 Apr 21;118(8):1861-1875. doi: 10.1016/j.bpj.2020.03.011. Epub 2020 Mar 29.
10
Gγ and Gα Identity Dictate a G-Protein Heterotrimer Plasma Membrane Targeting.Gγ 和 Gα 身份决定 G 蛋白异三聚体质膜靶向。
Cells. 2019 Oct 13;8(10):1246. doi: 10.3390/cells8101246.
本文引用的文献
1
Homo-FRET imaging enables quantification of protein cluster sizes with subcellular resolution.同型荧光共振能量转移（Homo-FRET）成像技术可实现亚细胞分辨率下对蛋白质簇大小的定量。
Biophys J. 2009 Nov 4;97(9):2613-22. doi: 10.1016/j.bpj.2009.07.059.
2
Fluorescent proteins for single-molecule fluorescence applications.用于单分子荧光应用的荧光蛋白。
J Biophotonics. 2008 Mar;1(1):74-82. doi: 10.1002/jbio.200710024.
3
Quantitative FRET analysis with the EGFP-mCherry fluorescent protein pair.使用EGFP-mCherry荧光蛋白对进行定量荧光共振能量转移分析。
Photochem Photobiol. 2009 Jan-Feb;85(1):287-97. doi: 10.1111/j.1751-1097.2008.00435.x. Epub 2008 Aug 27.
4
Improved monomeric red, orange and yellow fluorescent proteins derived from Discosoma sp. red fluorescent protein.源自盘状珊瑚红色荧光蛋白的改良单体红色、橙色和黄色荧光蛋白。
Nat Biotechnol. 2004 Dec;22(12):1567-72. doi: 10.1038/nbt1037. Epub 2004 Nov 21.
5
Förster distances between green fluorescent protein pairs.绿色荧光蛋白对之间的Förster距离。
Anal Biochem. 2000 Sep 10;284(2):438-40. doi: 10.1006/abio.2000.4708.
Zotero 插件