ESR reveals the mobility of the neck linker in dimeric kinesin

@article{citeulike:1391640, abstract = {Conventional kinesin is a highly processive motor that converts the chemical energy of ATP hydrolysis into the unidirectional motility along microtubules. The processivity is thought to depend on the coordination between ATPase cycles of two motor domains and their neck linkers. Here we have used site-directed spin labeling electron spin resonance (SDSL-ESR) to determine the conformation of the neck linker in kinesin dimer in the presence and absence of microtubules. The spectra show that the neck linkers co-exist in both docked and disordered conformations, which is consistent with the results of monomeric kinesin [Nat. Struct. Biol. 9 (2002) 844]. In all nucleotide states, however, the neck linkers are well ordered when dimeric kinesin is bound to the microtubule. This result suggests that the orientation of each neck linker that is fixed rigidly controls the kinesin motion along microtubule tracks.}, author = {Sugata, Kazunori and Nakamura, Motoyoshi and Ueki, Shoji and Fajer, Peter G. and Arata, Toshiaki }, citeulike-article-id = {1391640}, journal = {Biochemical and Biophysical Research Communications}, keywords = {esr, experiment, kinesin, motor, mt}, month = {February}, number = {2}, pages = {447--451}, posted-at = {2007-06-15 10:25:04}, priority = {2}, title = {ESR reveals the mobility of the neck linker in dimeric kinesin}, url = {http://www.sciencedirect.com/science/article/B6WBK-4BCXJ2J-6/2/062d297a43ae125045a22c22d6c8c140}, volume = {314}, year = {2004} }

TY - JOUR ID - citeulike:1391640 L3 - citeulike-article-id:1391640 TI - ESR reveals the mobility of the neck linker in dimeric kinesin JF - Biochemical and Biophysical Research Communications VL - 314 IS - 2 SP - 447 EP - 451 N2 - Conventional kinesin is a highly processive motor that converts the chemical energy of ATP hydrolysis into the unidirectional motility along microtubules. The processivity is thought to depend on the coordination between ATPase cycles of two motor domains and their neck linkers. Here we have used site-directed spin labeling electron spin resonance (SDSL-ESR) to determine the conformation of the neck linker in kinesin dimer in the presence and absence of microtubules. The spectra show that the neck linkers co-exist in both docked and disordered conformations, which is consistent with the results of monomeric kinesin [Nat. Struct. Biol. 9 (2002) 844]. In all nucleotide states, however, the neck linkers are well ordered when dimeric kinesin is bound to the microtubule. This result suggests that the orientation of each neck linker that is fixed rigidly controls the kinesin motion along microtubule tracks. KW - esr KW - experiment KW - kinesin KW - motor KW - mt AU - Sugata, Kazunori AU - Nakamura, Motoyoshi AU - Ueki, Shoji AU - Fajer, Peter AU - Arata, Toshiaki PY - 2004/02/06/ UR - http://www.sciencedirect.com/science/article/B6WBK-4BCXJ2J-6/2/062d297a43ae125045a22c22d6c8c140 ER -