Studying DNA-protein interactions with single-molecule Forster resonance energy transfer

被引：10

作者：

Farooq, Shazia ^{[1
]}

Fijen, Carel ^{[1
]}

Hohlbein, Johannes ^{[1
]}

机构：

[1] Wageningen UR, Biophys Lab, Wageningen, Netherlands

来源：

PROTOPLASMA | 2014年 / 251卷 / 02期

关键词：

Single-molecule Forster resonance energy transfer; Fluorescence; Enzymes; DNA; DNA-protein interactions; RNA-POLYMERASE-II; PROBABILITY-DISTRIBUTION ANALYSIS; MULTIPARAMETER FLUORESCENCE DETECTION; ALTERNATING-LASER EXCITATION; NANO-POSITIONING SYSTEM; ATOMIC-FORCE MICROSCOPE; 3.3 ANGSTROM RESOLUTION; COLI REP HELICASE; ESCHERICHIA-COLI; STRUCTURAL BASIS;

D O I：

10.1007/s00709-013-0596-6

中图分类号：

Q94 [植物学];

学科分类号：

071001 ;

摘要：

Single-molecule Forster resonance energy transfer (smFRET) has emerged as a powerful tool for elucidating biological structure and mechanisms on the molecular level. Here, we focus on applications of smFRET to study interactions between DNA and enzymes such as DNA and RNA polymerases. SmFRET, used as a nanoscopic ruler, allows for the detection and precise characterisation of dynamic and rarely occurring events, which are otherwise averaged out in ensemble-based experiments. In this review, we will highlight some recent developments that provide new means of studying complex biological systems either by combining smFRET with force-based techniques or by using data obtained from smFRET experiments as constrains for computer-aided modelling.

引用

页码：317 / 332

页数：16

共 50 条

[31] Single-molecule analysis of DNA-protein complexes using nanopores
Hornblower B.
Coombs A.
Whitaker R.D.
Kolomeisky A.
Picone S.J.
Meller A.
Akeson M.
Nature Methods, 2007, 4 (4) : 315 - 317
[32] COMBINING OPTICAL TWEEZERS, SINGLE-MOLECULE FLUORESCENCE MICROSCOPY, AND MICROFLUIDICS FOR STUDIES OF DNA-PROTEIN INTERACTIONS
Gross, Peter
Farge, Geraldine
Peterman, Erwin J. G.
Wuite, Gijs J. L.
METHODS IN ENZYMOLOGY, VOL 475: SINGLE MOLECULE TOOLS, PT B: SUPER-RESOLUTION, PARTICLE TRACKING, MULTIPARAMETER, AND FORCE BASED METHODS, 2010, 475 : 427 - 453
[33] Utilizing Biotinylated Proteins Expressed in Yeast to Visualize DNA-Protein Interactions at the Single-Molecule Level
Xue, Huijun
Bei, Yuanyuan
Zhan, Zhengyan
Chen, Xiuqiang
Xu, Xin
Fu, Yu V.
FRONTIERS IN MICROBIOLOGY, 2017, 8
[34] High-throughput single-molecule analysis of DNA-protein interactions by tethered particle motion
Plenat, Thomas
Tardin, Catherine
Rousseau, Philippe
Salome, Laurence
NUCLEIC ACIDS RESEARCH, 2012, 40 (12)
[35] Single-molecule DNA damage recognition: DNA-protein protein-protein interaction dynamics
Lu, HP
Iakoucheva, LM
Ackerman, EJ
BIOPHYSICAL JOURNAL, 2000, 78 (01) : 262A - 262A
[36] Plasmon-assisted Forster resonance energy transfer at the single-molecule level in the moderate quenching regime
Bohlen, J.
Cuartero-Gonzalez, A.
Pibiri, E.
Ruhlandt, D.
Fernandez-Dominguez, A., I
Tinnefeld, P.
Acuna, G. P.
NANOSCALE, 2019, 11 (16) : 7674 - 7681
[37] Genetically Encoded Forster Resonance Energy Transfer-Based Biosensors Studied on the Single-Molecule Level
Hoefig, Henning
Otten, Julia
Steffen, Victoria
Pohl, Martina
Boersma, Arnold J.
Fitter, Joerg
ACS SENSORS, 2018, 3 (08): : 1462 - 1470
[38] Quantifying kinetics from time series of single-molecule Forster resonance energy transfer efficiency histograms
Benke, Stephan
Nettels, Daniel
Hofmann, Hagen
Schuler, Benjamin
NANOTECHNOLOGY, 2017, 28 (11)
[39] Single-Molecule Forster Resonance Energy Transfer-Based Photosensitizer for Synergistic Photodynamic/Photothermal Therapy
Zou, Yang
Long, Saran
Xiong, Tao
Zhao, Xueze
Sun, Wen
Du, Jianjun
Fan, Jiangli
Peng, Xiaojun
ACS CENTRAL SCIENCE, 2021, 7 (02) : 327 - 334
[40] Quantitative Single-Molecule Three-Color Forster Resonance Energy Transfer by Photon Distribution Analysis
Barth, Anders
von Voithenberg, Lena Voith
Lamb, Don C.
JOURNAL OF PHYSICAL CHEMISTRY B, 2019, 123 (32): : 6901 - 6916

← 1 2 3 4 5 →