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We developed Linear Zero Mode Waveguides (LZMWs) for simultaneous observation of kinesin displacement and ATP hydrolysis cycle under higher concentration of fluorescently labeled ATP than that used in conventional total internal reflection microscopy (TIRFM). Single-molecule fluorescent microscopy is a promising method to analyze correlation between the mechanical displacement and hydrolysis of ATP...
For the analysis of kinesin motility, we demonstrate an observation system to simultaneously visualize kinesin and ATP molecules at the single molecule level using Linear Zero-Mode Waveguides (LZMWs). LZMWs allow fluorescent imaging at up to micromolar concentration by confining the excitation volume, which is high enough for studying enzymatic reactions such as ATP hydrolysis. LZMWs were fabricated...
Kinesin advances 8 nm along a microtubule per ATP hydrolyzed, but the mechanism responsible for coordinating the enzymatic cycles of kinesin's two identical motor domains remains unresolved. Here, we have tested whether such coordination is mediated by intramolecular tension generated by the “neck linkers,” mechanical elements that span between the motor domains. When tension is reduced by extending...
Unc104 (KIF1A) kinesin transports membrane vesicles along microtubules in lower and higher eukaryotes. Using an in vitro motility assay, we show that Unc104 uses a lipid binding pleckstrin homology (PH) domain to dock onto membrane cargo. Through its PH domain, Unc104 can transport phosphatidylinositol(4,5)bisphosphate (PtdIns(4,5)P 2 )-containing liposomes with similar properties to native...
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