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Effects of iodide on the coupling between ATP hydrolysis and motile activity in axonemal dynein.

机译：碘化物对AxoNemal Dynein中ATP水解与电动活性的偶联的影响。

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摘要

Dynein transduces the chemical energy of ATP hydrolysis into mechanical work through conformational changes. To identify the factors governing the coupling between the ATPase activity and the motile activity of the dynein molecule, we examined the effects of potassium iodide, which can unfold protein tertiary structures, on dynein activity in reactivated sea urchin sperm flagella. The presence of low concentrations of KI (0.05-0.1 M) in the reactivating solution did not influence the stable beating of demembranated flagella at 0.02-1 mM ATP, when the total concentration of potassium was kept at 0.15 M by adding K-acetate. However, double-reciprocal plots of ATP concentration and beat frequency showed a mixed type of inhibition by KI, indicating the possibility that KI inhibits the ATP hydrolysis and decreases the maximum sliding velocity. The ATPase activity of 21S dynein with or without microtubules did not decrease with the KI concentration. In the elastase-treated axonemes, KI decreased the velocity of sliding disintegration, while it increased the frequency of occurrence of axonemes showing no sliding. This may be related to some defect in the coordination of dynein activities. On 21S dynein adsorbed on a glass surface, however, the velocity of microtubule sliding was increased by KI, while KI lowered the dynein-microtubule affinity. The velocity further increased under lower salt conditions enhancing the dynein-microtubule interactions. The results suggest the importance of organized regulation of the dynamic states of dynein-microtubule interactions through the stalk for the coupling between the ATPase activity and the motile activity of dynein in beating flagella.
机译：Dynein通过构象变化将ATP水解的化学能转换为机械工作。为了鉴定治疗当时分子的ATP酶活性和动机活性的偶联的因素，我们研究了碘化钾的作用，该碘化钾可以展开蛋白质三级结构，在重新激活的海胆鞭毛中的Dynein活性上。重新激活溶液中低浓度的Ki（0.05-0.1M）的存在在0.02-1mm ATP时不会影响稳定的鞭毛，当通过加入k-乙酸钾将钾的总浓度保持在0.15μm时。然而，ATP浓度和拍频的双倒数曲线曲线表现出Ki的混合抑制类型，表明Ki抑制ATP水解的可能性并降低最大滑动速度。 21s Dynein的ATPase活性与微管或没有微管的ATP酶活性没有随着Ki浓度降低。在弹性酶处理的轴突中，ki降低了滑动崩解的速度，而它增加了轴突的发生频率，显示不显示滑动。这可能与某些缺陷有关的Dynin活动的协调。然而，在21S上吸附在玻璃表面上的Dynein，通过Ki增加了微管滑动的速度，而Ki降低了Dynein-Micro管亲和力。在较低盐条件下进一步增加了速度，增强了Dynein-微管相互作用。结果表明，通过茎干通过秸秆与抗鞭毛中Dynein之间的偶联的偶联的偶联的动态调节动态调节动态调节。

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