Capelli N, Barja F, van Tuinen D, Monnat J, Turian G, Ortega Perez R
Laboratory of Biochemistry and Plant Physiology, University of Geneva, Switzerland.
FEMS Microbiol Lett. 1997 Feb 15;147(2):215-20. doi: 10.1111/j.1574-6968.1997.tb10244.x.
We have enriched a 47-kDa polypeptide (p47) from Neurospora crassa on the basis of its affinity to calmodulin. The p47 was purified to homogeneity by chromatography on a Mono S cation exchange column and evidence is presented that the polypeptide co-sediments specifically with F-actin. The intracellular distribution of p47 and actin was also examined using indirect double immunofluorescence staining of cells at different stages of development. Our results suggest that by altering the conformation binding site of actin to p47, calmodulin could play a regulatory role in the polarized hyphal growth of N. crassa.
我们基于其与钙调蛋白的亲和力，从粗糙脉孢菌中富集了一种47 kDa的多肽（p47）。通过在Mono S阳离子交换柱上进行色谱分离，将p47纯化至同质状态，并提供了该多肽与F-肌动蛋白特异性共沉降的证据。还使用不同发育阶段细胞的间接双重免疫荧光染色检查了p47和肌动蛋白的细胞内分布。我们的结果表明，通过改变肌动蛋白与p47的构象结合位点，钙调蛋白可能在粗糙脉孢菌的极化菌丝生长中发挥调节作用。
