ORIENTATION OF ACTIN-FILAMENTS DURING MOTION IN IN-VITRO MOTILITY ASSAY
ORIENTATION OF ACTIN-FILAMENTS DURING MOTION IN IN-VITRO MOTILITY ASSAY
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DOI：
10.1016/s0006-3495(94)80946-4
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发表时间：
1994-05-01
影响因子：
3.4
通讯作者：
BURLACU, S
中科院分区：
文献类型：
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作者：
BOREJDO, J;BURLACU, S
将罗丹明鬼笔环肽加入到F-肌动蛋白中，用荧光偏振法测量了染料的过渡偶极在单个肌动蛋白丝上的取向。罗丹明鬼笔环肽被很好地固定在肌动蛋白的表面上，表明染料的取向变化报告了肌动蛋白单体的取向变化。在静止的灯丝中，偶极子相对于灯丝轴倾斜49.3度。静止细丝中偶极的解体并不明显。当长丝被平移时，染料的平均取向没有改变，但无序性略有增加。当细丝在溶液中游离时，组织解体显著增加。我们的结论是，在我们的测量精度（约18%），肌动蛋白单体在运动过程中没有发生重大的重新取向，但肌球蛋白头的结合变形的细丝的结构。
Rhodamine-phalloidin was added to F-actin, and the orientation of transition dipoles of the dye was measured single actin filaments by polarization of fluorescence. Rhodamine-phalloidin was well immobilized on the surface of actin, indicating that changes in orientation of the dye reported changes in orientation of actin monomers. In stationary filaments the dipoles were inclined at 49.3 degrees with respect to the filament axis. The disorganization of dipoles in stationary filaments was insignificant. When the filaments were made to translate, the average orientation of the dye did not change, but disorganization slightly increased. Disorganization increased significantly when filaments were free in solution. We concluded that, within the accuracy of our measurements (approximate to 18%), actin monomers did not undergo major reorientations during motion, but that binding of myosin heads deformed the structure of filaments.