Fowler V M
Department of Molecular Biology, Research Institute of Scripps Clinic, La Jolla, California 92041.
J Cell Biol. 1990 Aug;111(2):471-81. doi: 10.1083/jcb.111.2.471.
Human erythrocytes contain a Mr 43,000 tropomyosin-binding protein that is unrelated to actin and that has been proposed to play a role in modulating the association of tropomyosin with spectrin-actin complexes based on its stoichiometry in the membrane skeleton of one Mr 43,000 monomer per short actin filament (Fowler, V. M. 1987. J. Biol. Chem. 262:12792-12800). Here, we describe an improved procedure to purify milligram quantities to 98% homogeneity and we show that this protein inhibits tropomyosin binding to actin by a novel mechanism. We have named this protein tropomodulin. Unlike other proteins that inhibit tropomyosin-actin interactions, tropomodulin itself does not bind to F-actin. EM of rotary-shadowed tropomodulin-tropomyosin complexes reveal that tropomodulin (14.5 +/- 2.4 nm [SD] in diameter) binds to one of the ends of the rod-like tropomyosin molecules (33 nm long). In agreement with this observation, Dixon plots of inhibition curves demonstrate that tropomodulin is a non-competitive inhibitor of tropomyosin binding to F-actin (Ki = 0.7 microM). Hill plots of the binding of the tropomodulin-tropomyosin complex to actin indicate that binding does not exhibit any positive cooperativity (n = 0.9), in contrast to tropomyosin (n = 1.9), and that the apparent affinity of the complex for actin is reduced 20-fold with respect to that of tropomyosin. These results suggest that binding of tropomodulin to tropomyosin may block the ability of tropomyosin to self-associate in a head-to-tail fashion along the actin filament, thereby weakening its binding to actin. Antibodies to tropomodulin cross-react strongly with striated muscle troponin I (but not with troponin T) as well as with a nontroponin Mr 43,000 polypeptide in muscle and in other nonerythroid cells and tissues, including brain, lens, neutrophils, and endothelial cells. Thus, erythrocyte tropomodulin may be one member of a family of tropomyosin-binding proteins that function to regulate tropomyosin-actin interactions in non-muscle cells and tissues.
人类红细胞含有一种分子量为43,000的原肌球蛋白结合蛋白,它与肌动蛋白无关,基于其在膜骨架中每短肌动蛋白丝一个分子量为43,000的单体的化学计量比,有人提出它在调节原肌球蛋白与血影蛋白 - 肌动蛋白复合物的结合中起作用(福勒,V.M. 1987.《生物化学杂志》262:12792 - 12800)。在此,我们描述了一种改进的纯化方法,可将毫克量的该蛋白纯化至98%的纯度,并且我们表明这种蛋白通过一种新机制抑制原肌球蛋白与肌动蛋白的结合。我们将这种蛋白命名为原肌球蛋白调节蛋白。与其他抑制原肌球蛋白 - 肌动蛋白相互作用的蛋白不同,原肌球蛋白调节蛋白本身不与F - 肌动蛋白结合。旋转阴影的原肌球蛋白调节蛋白 - 原肌球蛋白复合物的电子显微镜观察显示,原肌球蛋白调节蛋白(直径为14.5±2.4纳米[标准差])结合到杆状原肌球蛋白分子(33纳米长)的一端。与这一观察结果一致,抑制曲线的迪克森图表明原肌球蛋白调节蛋白是原肌球蛋白结合F - 肌动蛋白的非竞争性抑制剂(Ki = 0.7微摩尔)。原肌球蛋白调节蛋白 - 原肌球蛋白复合物与肌动蛋白结合的希尔图表明,与原肌球蛋白(n = 1.9)相反,该结合不表现出任何正协同性(n = 0.9),并且该复合物对肌动蛋白的表观亲和力相对于原肌球蛋白降低了20倍。这些结果表明,原肌球蛋白调节蛋白与原肌球蛋白的结合可能会阻止原肌球蛋白沿肌动蛋白丝以头对尾的方式自我缔合的能力,从而削弱其与肌动蛋白的结合。抗原肌球蛋白调节蛋白的抗体与横纹肌肌钙蛋白I(但不与肌钙蛋白T)以及肌肉和其他非红细胞的细胞及组织(包括脑、晶状体、中性粒细胞和内皮细胞)中的一种非肌钙蛋白分子量为43,000的多肽发生强烈交叉反应。因此,红细胞原肌球蛋白调节蛋白可能是原肌球蛋白结合蛋白家族的一员,该家族在非肌肉细胞和组织中发挥调节原肌球蛋白 - 肌动蛋白相互作用的功能。