INTERRELATIONSHIPS BETWEEN THERMAL, N-ETHYLMALEIMIDE, AND CA2+-CALMODULIN-MEDIATED ACTIVATION-INACTIVATION OF DYNEIN ATPASE ACTIVITIES
INTERRELATIONSHIPS BETWEEN THERMAL, N-ETHYLMALEIMIDE, AND CA2+-CALMODULIN-MEDIATED ACTIVATION-INACTIVATION OF DYNEIN ATPASE ACTIVITIES
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DOI：
10.1016/0003-9861(81)90199-5
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发表时间：
1981-01-01
影响因子：
3.9
通讯作者：
VANAMAN, TC
中科院分区：
文献类型：
--
作者：
BLUM, JJ;HAYES, A;VANAMAN, TC
[使用梨形四膜虫的纤毛]研究了钙调素激活30 S动力蛋白ATP酶活性与热或N-乙基马来酰亚胺（NEM）激活之间的相互作用。在热处理过程中加入钙调素引起的ATP酶活性的增加（以上所造成的单独加热）比热处理后加入钙调素。在由NEM [N-乙基马来酰亚胺]处理引起活化的实验中获得了类似的结果。对于热和NEM处理，钙调蛋白的协同作用时，在治疗过程中存在的是Ca 2+依赖性的，虽然激活的ATP酶活性，由任一单独的治疗是不依赖于Ca 2+。加热14 S动力蛋白抑制其ATP酶活性，并降低钙调素作为激活剂的有效性。在加热或NEM处理后加入的钙调蛋白的活化效果与处理期间存在钙调蛋白的情况大致相同，即，互动影响很小。对14 S动力蛋白ATP酶活性影响不大的NEM浓度在很大程度上消除了钙调蛋白激活其ATP酶活性的能力。热处理后的14 S动力蛋白在钙调素-Sepharose 4 B上的层析表明，14 S动力蛋白ATP酶对钙调素的敏感性的丧失不是由于动力蛋白与钙调素结合能力的丧失。热处理的30 S动力蛋白也显示出钙调蛋白结合能力的保留。钙调素和热/NEM可能激活增溶的30 S动力蛋白ATP酶通过不同的机制，其中可能包括一个共同的过程。
Interactive effects between calmodulin activation of 30 S dynein ATPase activity and activation by heat or N-ethylmaleimide (NEM) were studied [using cilia from Tetrahymena pyriformis]. Addition of calmodulin during the heat treatment caused a larger increment in ATPase activity (above that caused by heating alone) than did addition of calmodulin after the heat treatment. Similar results were obtained in experiments where activation was caused by NEM [N-ethylmaleimide] treatment. For the heat and NEM treatments, the synergistic effect of calmodulin when present during the treatment was Ca2+ dependent although activation of ATPase activity by either treatment alone was not Ca2+ dependent. Heating 14 S dynein inhibited its ATPase activity and reduced the effectiveness of calmodulin as an activator. The activating effect of calmodulin added after heat or NEM treatment was about the same as if the calmodulin was present during the treatment, i.e., interactive effects were minimal. Concentrations of NEM that had little effect on the ATPase activity of 14 S dynein largely eliminated the ability of calmodulin to activate its ATPase activity. Chromatography of the heat-treated 14 S dynein on calmodulin-Sepharose 4B indicated that the loss of sensitivity of 14 S dynein ATPase to calmodulin was not due to loss of ability of the dynein to bind to calmodulin. Retention of calmodulin binding ability was also shown for heat-treated 30 S dynein. Calmodulin and heat/NEM probably activate solubilized 30 S dynein ATPase by separate mechanisms which may include a common process.