Recent advances in FRET: distance determination in protein-DNA complexes

被引：151

作者：

Hillisch, A

Lorenz, M

Diekmann, S

机构：

[1] EnTec GmbH, D-07745 Jena, Germany

[2] Inst Mol Biotechnol, D-07745 Jena, Germany

来源：

CURRENT OPINION IN STRUCTURAL BIOLOGY | 2001年 / 11卷 / 02期

关键词：

D O I：

10.1016/S0959-440X(00)00190-1

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Fluorescence resonance energy transfer (FRET) provides information on the distance between a donor and an acceptor dye in the range 10 to 100 Angstrom. Knowledge of the exact positions of some dyes with respect to nucleic acids now enables us to translate these data into precise structural information using molecular modeling. Advances in the preparation of dye-labeled nucleic acid molecules and in new techniques, such as the measurement of FRET in polyacrylamide gels or in vivo, will lead to an increasingly important role of FRET in structural and molecular biology.

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收藏

页码：201 / 207

页数：7

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共 60 条

[31] Dynamic and quantitative Ca2+ measurements using improved cameleons [J].

Miyawaki, A ;

Griesbeck, O ;

Heim, R ;

Tsien, RY .

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1999, 96 (05) :2135-2140

[32] Fluorescent indicators for Ca2+ based on green fluorescent proteins and calmodulin [J].

Miyawaki, A ;

Llopis, J ;

Heim, R ;

McCaffery, JM ;

Adams, JA ;

Ikura, M ;

Tsien, RY .

NATURE, 1997, 388 (6645) :882-887

[33] The structure of a chromosomal high mobility group protein-DNA complex reveals sequence-neutral mechanisms important for non-sequence-specific DNA recognition [J].

Murphy, FV ;

Sweet, RM ;

Churchill, MEA .

EMBO JOURNAL, 1999, 18 (23) :6610-6618

[34] Location of cyanine-3 on double-stranded DNA:: Importance for fluorescence resonance energy transfer studies [J].

Norman, DG ;

Grainger, RJ ;

Uhrín, D ;

Lilley, DMJ .

BIOCHEMISTRY, 2000, 39 (21) :6317-6324

[35] Basis for recognition of cisplatin-modified DNA by high-mobility-group proteins [J].

Ohndorf, UM ;

Rould, MA ;

He, Q ;

Pabo, CO ;

Lippard, SJ .

NATURE, 1999, 399 (6737) :708-712

[36] Determination of interactions between structured nucleic acids by fluorescence resonance energy transfer (FRET): selection of target sites for functional nucleic acids [J].

Ota, N ;

Hirano, K ;

Warashina, M ;

Andrus, A ;

Mullah, B ;

Hatanaka, K ;

Taira, K .

NUCLEIC ACIDS RESEARCH, 1998, 26 (03) :735-743

[37] Detection of DNA bending in a DNA-PAP1 protein complex by fluorescence resonance energy transfer [J].

Ozaki, H ;

Iwase, N ;

Sawai, H ;

Kodama, T ;

Kyogoku, Y .

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 1997, 231 (03) :553-556

[38] Intermediate species possessing bent DNA are present along the pathway to formation of a final TBP-TATA complex [J].

Parkhurst, KM ;

Richards, RM ;

Brenowitz, M ;

Parkhurst, LJ .

JOURNAL OF MOLECULAR BIOLOGY, 1999, 289 (05) :1327-1341

[39] Simultaneous binding and bending of promoter DNA by the TATA binding protein: Real time kinetic measurements [J].

Parkhurst, KM ;

Brenowitz, M ;

Parkhurst, LJ .

BIOCHEMISTRY, 1996, 35 (23) :7459-7465

[40] The structure of a CAP-DNA complex having two cAMP molecules bound to each monomer [J].

Passner, JM ;

Steitz, TA .

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1997, 94 (07) :2843-2847

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