Reversible control of F1-ATPase rotational motion using a photochromic ATP analog at the single moecule level
Reversible control of F1-ATPase rotational motion using a photochromic ATP analog at the single moecule level
复制标题
使用光致变色 ATP 类似物在单分子水平可逆控制 F1-ATPase 旋转运动
DOI：
10.1016/j.bbrc.2014.02.117
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发表时间：
2014
期刊：
影响因子：
--
通讯作者：
T.
中科院分区：
文献类型：
--
作者：
Sunamura;E.;Kamei;K.;Konno;H.;Tamaoki;N.;Hisabori;T.
运动酶如F1-ATP酶和驱动蛋白利用ATP的能量进行运动。这些酶的分子运动是其催化机制的关键，并使用单分子观察技术进行了彻底的分析。作为一种分析和控制ATP驱动的运动酶运动的工具，我们最近合成了一种光敏ATP类似物，其在核糖环的2′位上连接有对叔丁基偶氮苯。利用偶氮苯部分的顺式/反式异构化，我们成功地实现了对驱动蛋白-微管系统的可逆光致变色控制。在这里，我们成功地控制水解活性和旋转马达酶，F1-ATP酶，使用这种光敏ATP类似物的旋转。随后的单分子观察表明，在类似物的顺式存在下，在ATP结合角位置处发生独特的暂停。
Motor enzymes such as F1-ATPase and kinesin utilize energy from ATP for their motion. Molecular motions of these enzymes are critical to their catalytic mechanisms and were analyzed thoroughly using a single molecule observation technique. As a tool to analyze and control the ATP-driven motor enzyme motion, we recently synthesized a photoresponsive ATP analog with ap-tert-butylazobenzene tethered to the 2′ position of the ribose ring. Usingcis/transisomerization of the azobenzene moiety, we achieved a successful reversible photochromic control over a kinesin-microtubule system in anin vitromotility assay. Here we succeeded to control the hydrolytic activity and rotation of the rotary motor enzyme, F1-ATPase, using this photosensitive ATP analog. Subsequent single molecule observations indicated a unique pause occurring at the ATP binding angle position in the presence ofcisform of the analog.