Shukla Vaibhav Kumar, Kabra Ashish, Yadav Rahul, Ono Shoichiro, Kumar Dinesh, Arora Ashish
Molecular and Structural Biology Division, CSIR-Central Drug Research Institute, Lucknow, 226 031, India.
Department of Pathology, Emory University, Atlanta, GA, 30322, USA.
Biomol NMR Assign. 2015 Oct;9(2):261-5. doi: 10.1007/s12104-014-9588-5. Epub 2014 Dec 11.
The actin filament dynamics in nematode, Caenorhabditis elegans, is regulated by differential activity of two proteins UNC-60A and UNC-60B. UNC-60A exhibits strong pointed end depolymerization on C. elegans actin (Ce-actin), strong inhibition of polymerization, strong monomer sequestering activity, weak severing activity, and low affinity for F-actin binding, while UNC-60B exhibits strong pointed end depolymerization on rabbit muscle actin, strong severing activity, and high affinity for F-actin binding. Structural characterization of these proteins will help to understand (1) molecular mechanism of actin dynamics regulation and (2) the differential activity of these proteins. Here, we report (1)H, (13)C, and (15)N chemical shift assignments of these two proteins as determined by heteronuclear NMR experiments (at pH 6.5 and temperature 298 K).
线虫秀丽隐杆线虫中的肌动蛋白丝动力学受两种蛋白质UNC-60A和UNC-60B的不同活性调节。UNC-60A对线虫肌动蛋白（Ce-肌动蛋白）表现出强烈的尖端解聚、对聚合的强烈抑制、强烈的单体隔离活性、较弱的切断活性以及对F-肌动蛋白结合的低亲和力，而UNC-60B对兔肌肌动蛋白表现出强烈的尖端解聚、强烈的切断活性以及对F-肌动蛋白结合的高亲和力。这些蛋白质的结构表征将有助于理解（1）肌动蛋白动力学调节的分子机制以及（2）这些蛋白质的不同活性。在此，我们报告了通过异核NMR实验（在pH 6.5和温度298 K下）确定的这两种蛋白质的（1）H、（13）C和（15）N化学位移归属。
