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Literature DB >> 28940071

Use of Single Molecule Fluorescence Polarization Microscopy to Study Protein Conformation and Dynamics of Kinesin-Microtubule Complexes.

Abstract

Single molecule fluorescence polarization microscopy (smFPM) is a technique that enables to monitor changes in the orientation of a single labeled protein domain. Here we describe a smFPM microscope set-up and protocols to investigate conformational changes associated with the movement of motor proteins along cytoskeletal tracks.

Entities: CellLine Chemical Disease Gene Species

Keywords: BSR; Dichroism; Fluorescence polarization; Kinesin; Microtubule; Molecular motor; Single molecule

Mesh：

Substances：

Year: 2018 PMID： 28940071 PMCID： PMC5760212 DOI： 10.1007/978-1-4939-7271-5_11

Source DB: PubMed Journal: Methods Mol Biol ISSN： 1064-3745

20 in total

1. Stepping rotation of F1-ATPase visualized through angle-resolved single-fluorophore imaging.

Authors: K Adachi; R Yasuda; H Noji; H Itoh; Y Harada; M Yoshida; K Kinosita
Journal: Proc Natl Acad Sci U S A Date: 2000-06-20 Impact factor: 11.205

Review 2. Single-molecule fluorescence spectroscopy and microscopy of biomolecular motors.

Authors: Erwin J G Peterman; Hernando Sosa; W E Moerner
Journal: Annu Rev Phys Chem Date: 2004 Impact factor: 12.703

Review 3. Fluorescence polarization microscopy.

Authors: D Axelrod
Journal: Methods Cell Biol Date: 1989 Impact factor: 1.441

4. Kinesin moving through the spotlight: single-motor fluorescence microscopy with submillisecond time resolution.

Authors: Sander Verbrugge; Lukas C Kapitein; Erwin J G Peterman
Journal: Biophys J Date: 2007-01-19 Impact factor: 4.033

5. Configuration of the two kinesin motor domains during ATP hydrolysis.

Authors: Ana B Asenjo; Natan Krohn; Hernando Sosa
Journal: Nat Struct Biol Date: 2003-09-14

Review 6. Future challenges in single-molecule fluorescence and laser trap approaches to studies of molecular motors.

Authors: Mary Williard Elting; James A Spudich
Journal: Dev Cell Date: 2012-12-11 Impact factor: 12.270

Review 7. Structure and dynamics of the kinesin-microtubule interaction revealed by fluorescence polarization microscopy.

Authors: Hernando Sosa; Ana B Asenjo; Erwin J G Peterman
Journal: Methods Cell Biol Date: 2010 Impact factor: 1.441

Use of Single Molecule Fluorescence Polarization Microscopy to Study Protein Conformation and Dynamics of Kinesin-Microtubule Complexes.

1. Stepping rotation of F1-ATPase visualized through angle-resolved single-fluorophore imaging.

Review 2. Single-molecule fluorescence spectroscopy and microscopy of biomolecular motors.

Review 3. Fluorescence polarization microscopy.

4. Kinesin moving through the spotlight: single-motor fluorescence microscopy with submillisecond time resolution.

5. Configuration of the two kinesin motor domains during ATP hydrolysis.

Review 6. Future challenges in single-molecule fluorescence and laser trap approaches to studies of molecular motors.

Review 7. Structure and dynamics of the kinesin-microtubule interaction revealed by fluorescence polarization microscopy.

8. An oxygen scavenging system for improvement of dye stability in single-molecule fluorescence experiments.

9. Elongation factor G initiates translocation through a power stroke.

10. Distinct Interaction Modes of the Kinesin-13 Motor Domain with the Microtubule.

Review 1. Fluorescence microscopy applied to intracellular transport by microtubule motors.

2. Single molecule turnover of fluorescent ATP by myosin and actomyosin unveil elusive enzymatic mechanisms.

3. Multistep orthophosphate release tunes actomyosin energy transduction.