An alpha-actinin-profilin chimaera with two alternatively operatingactin-binding sites

Schluter K.; Zeuschner D.; Winkler J.; Pope B.; Weeds A.; Jockusch BM.

首页> 外文期刊>European Journal of Cell Biology: Journal of Deutsche Gesellschaft fur Elektronenmikroskopie: Journal of Deutsche Gesellschaft fur Zellbiologie >An alpha-actinin-profilin chimaera with two alternatively operatingactin-binding sites

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An alpha-actinin-profilin chimaera with two alternatively operatingactin-binding sites

机译：α-actinin-profilinchimaera具有两个交替操作的actin结合位点

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Studying the mode of interaction between actin and actin-binding proteins, we constructed a chimaeric protein consisting of the sequence for bovine profilin I (P), to which the sequence for the actin-binding domain of Dictyostelium discoideum alpha-actinin (alpha AP-2) was fused N-terminally. The resulting hybrid clone was expressed in Escherichia coli, and the chimaeric protein, alpha A1-2P, purified by affinity chromatography on poly-(L-proline) (PLP) columns and identified using specific antibodies. High resolution electron microscopy demonstrated that this protein consists of two discrete subdomains. In biochemical, viscometric and electron microscopic analyses, we shelved that both modules in this molecule are biologically active. The chimaera binds to poly-(L-proline) and inhibits the polymerization of G-actin in KCI, which is consistent with the assumption that the profilin part is intact. Inhibition of actin polymerization in KCI was stronger than that of the parental profilin, and the K-d value of its interaction with rabbit skeletal muscle actin, as determined by falling ball viscometry, was smaller (mean value 0.5 x 10(-6) M, as compared to 1.9 x 10(-6) M for bovine profilin).

机译：研究肌动蛋白与肌动蛋白结合蛋白之间的相互作用模式，我们构建了一种嵌合蛋白，由牛纤溶酶I（P）的序列组成，盘基网柄菌α-肌动蛋白（αAP- 2）N端融合。所得的杂种克隆在大肠杆菌中表达，并通过聚-（L-脯氨酸）（PLP）色谱柱上的亲和色谱法纯化嵌合蛋白αA1-2P，并使用特异性抗体进行鉴定。高分辨率电子显微镜证明该蛋白由两个离散的亚结构域组成。在生化，粘度和电子显微镜分析中，我们搁置了该分子中的两个模块都具有生物活性。该嵌合体与聚-（L-脯氨酸）结合并抑制KCI中G-肌动蛋白的聚合，这与脯氨酸蛋白部分完整的假设是一致的。肌动蛋白在KCI中的抑制作用要强于亲本的profilin，通过落球粘度法测定，其与兔骨骼肌肌动蛋白相互作用的Kd值较小（平均值为0.5 x 10（-6）M，与1.9 x 10（-6）M的牛蛋白原相比）。

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《European Journal of Cell Biology: Journal of Deutsche Gesellschaft fur Elektronenmikroskopie: Journal of Deutsche Gesellschaft fur Zellbiologie》 |1998年第1期|共8页
作者
Schluter K.; Zeuschner D.; Winkler J.; Pope B.; Weeds A.; Jockusch BM.;
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正文语种 eng
中图分类细胞生物学;
关键词
Actin filaments; Actin-binding proteins; Viscometry; Electron; Amino-acid sequence; Acanthamoeba profilin; Electron-microscopy; Calf; spleen; Filaments; Nucleotide; Protein; Cells; Cytoskeleton; Cytokinesis;

机译：肌动蛋白丝;肌动蛋白结合蛋白;粘度法;电子;氨基酸序列;棘阿米巴原纤维蛋白;电子显微镜;小腿;脾脏;细丝;核苷酸;蛋白质;细胞;细胞骨架;细胞分裂;

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1. An alpha-actinin-profilin chimaera with two alternatively operatingactin-binding sites [J] . Schluter K., Zeuschner D., Winkler J., European Journal of Cell Biology: Journal of Deutsche Gesellschaft fur Elektronenmikroskopie: Journal of Deutsche Gesellschaft fur Zellbiologie . 1998,第1期

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2. Role of the branch site/3'-splice site region in adenovirus-2 E1A pre-mRNA alternative splicing: evidence for 5'- and 3'-splice site co-operation [J] . Goran Akusj?rvi, Jan-Peter Kreivi, Per Johan Ulfendahl Nucleic acids research . 1989,第3期

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7. Role of the branch site/3'-splice site region in adenovirus-2 E1A pre-mRNA alternative splicing: evidence for 5'- and 3'-splice site co-operation. [O] . Ulfendahl, P J, Kreivi, J P, Akusjärvi, G 1989

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An alpha-actinin-profilin chimaera with two alternatively operatingactin-binding sites

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