Vidali L, Pérez H E, Valdés López V, Noguez R, Zamudio F, Sánchez F
Departamento de Biología Molecular de Plantas, Universidad Nacional Autónoma de México, Cuernavaca, Morelos.
Plant Physiol. 1995 May;108(1):115-23. doi: 10.1104/pp.108.1.115.
Profilin from common bean (Phaseolus vulgaris L.) was purified to homogeneity by poly-L-Pro affinity chromatography and gel filtration. The hypocotyl and symbiotic root nodule protein was detected as a single isoform with a 14.4-kD molecular mass and an isoelectric point of 5.3. Partial amino acid and DNA sequencing of a full-length cDNA clone confirmed its identity as profilin. An antibody generated against the purified protein binds to a protein with the same molecular mass in leaves and nodules. Immunolocalization of the protein showed a diffuse distribution in the cytoplasm of hypocotyls and nodules but enhanced staining at the vascular bundles. The strong identity of the sequence among the profilins of birch, maize, and bean suggests that it may play an important role in the signal transduction mechanism of plant cells and plant-bacterial symbioses.
通过聚-L-脯氨酸亲和层析和凝胶过滤，将菜豆（Phaseolus vulgaris L.）中的肌动蛋白结合蛋白纯化至同质。下胚轴和共生根瘤蛋白被检测为单一异构体，分子量为14.4 kDa，等电点为5.3。全长cDNA克隆的部分氨基酸和DNA测序证实其为肌动蛋白结合蛋白。针对纯化蛋白产生的抗体与叶片和根瘤中分子量相同的蛋白结合。该蛋白的免疫定位显示，在下胚轴和根瘤的细胞质中呈弥散分布，但在维管束处染色增强。桦树、玉米和菜豆的肌动蛋白结合蛋白之间序列的高度一致性表明，它可能在植物细胞的信号转导机制以及植物-细菌共生中发挥重要作用。
