Motility of single one-headed kinesin molecules along microtubules

Biophysical Journal

Volumn 81, Issue 5, 2001, Pages 2838-2850

  Inoue, Yuichi ^a,d   Iwane, Atsuko Hikikoshi ^b   Miyai, Takayuki ^b   Muto, Etsuko ^c,e   Yanagida, Toshio ^a,b  

^a Japan Science and Technology Agency   (Japan)

^b OSAKA UNIVERSITY   (Japan)

^c JAPAN SCIENCE AND TECHNOLOGY AGENCY   (Japan)

^d UNIVERSITY OF TOKYO   (Japan)

^e RIKEN BRAIN SCIENCE INSTITUTE   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL ENZYME; CARBOXYLTRANSFERASE; KINESIN;

ARTICLE; CARBOXY TERMINAL SEQUENCE; DROSOPHILA; ENZYME BINDING; FLUORESCENCE MICROSCOPY; MEASUREMENT; MICROTUBULE; NONHUMAN; PROPIONIBACTERIUM FREUDENREICHII SHERMANII;

BACTERIA (MICROORGANISMS); PROPIONIBACTERIUM; PROPIONIBACTERIUM FREUDENREICHII SUBSP. SHERMANII;

EID: 0034765827     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(01)75925-5     Document Type: Article

References (40)

1. Failure of a single-headed kinesin to track parallel to microtubule protofilaments
2. Bead movement by single kinesin molecules studied with optical tweezers
3. The directional preference of kinesin motors is specified by an element outside of the motor catalytic domain
4. Sedimentation studies on the kinesin motor domain constructs K401, K366, and K341
5. On the hand-over-hand footsteps of kinesin heads
6. Determinants of kinesin motor polarity
7. Imaging of single fluorescent molecules and individual ATP turnovers by single myosin molecules in aqueous solution
8. Evidence for alternating head catalysis by kinesin during microtubule-stimulated ATP hydrolysis
9. Highly processive microtubule-stimulated ATP hydrolysis by dimeric kinesin head domains
10. Processivity of the motor protein kinesin requires two heads
11. Kinesin's processivity results from mechanical and chemical coordination between the ATP hydrolysis cycles of the two motor domains
12. Mechanochemical coupling in actomyosin energy transduction studied by in vitro movement assay
13. Reversal in the direction of movement of a molecular motor
14. Kinetics of force generation by single kinesin molecules activated by laser photolysis of caged ATP
15. Movement of microtubules by single kinesin molecules
16. Coupling of kinesin steps to ATP hydrolysis
17. Drosophila kinesin minimal motor domain expressed in Escherichia coll
18. Drosophila kinesin motor domain extending to amino acid position 392 is dimeric when expressed in Escherichia coli
19. Preparation of modified tubulins
20. Movements of truncated kinesin fragments with a short or an artificial flexible neck
21. Myosin subfragment-I is fully equipped with factors essential for motor function
22. Mechanical and chemical properties of cysteine-modified kinesin molecules
23. Influence of the kinesin neck domain on dimerization and ATPase kinetics
24. 15 Å resolution model of the monomeric kinesin motor, KIFIA
25. The crystal structure of dimeric kinesin and implications for microtubule-dependent motility
26. Crystal structure of the kinesin motor domain reveals a structural similarity to myosin
27. Kinetic mechanism of a monomeric kinesin construct
28. Direct inhibition of microtubule-based kinesin motility by local anesthetics
29. Purification and characterization of two monomeric kinesin constructs
30. A processive single-headed motor: Kinesin superfamily protein KIFIA
31. Mechanism of the single-headed processivity: Diffusional anchoring between the K-loop of kinesin and the C terminus of tubulin
32. Single-molecule behavior of monomeric and heteromeric kinesins
33. A structural change in the kinesin motor protein that drives motility
34. Role of the kinesin neck region in processive microtubule-based motility
35. X-ray structure of motor and neck domains from rat brain kinesin
36. Kinesin hydrolyses one ATP per 8-nm step
37. Direct observation of single kinesin molecules moving along microtubules
38. Release of isolated single kinesin molecules from microtubules
39. One-headed kinesin derivatives move by a nonprocessive, low-duty ratio mechanism unlike that of two-headed kinesin