Heintzelman M B, Frankel S A, Artavanis-Tsakonas S, Mooseker M S
Department of Biology, Yale University, New Haven, CT 06511.
J Mol Biol. 1993 Apr 5;230(3):709-16. doi: 10.1006/jmbi.1993.1191.
Gelsolin is an actin-binding protein with the abilities to sever and cap the barbed end of actin filaments and to promote the assembly of monomeric actin. It has been identified in vertebrates both as a cytoplasmic protein and as a protein secreted into the blood plasma. Here we report the nucleic acid sequence of the full-length complementary DNA for a secretory form of gelsolin from Drosophila. The deduced amino acid sequence of 790 residues (M(r) = 87,669) contains a predicted signal peptide of 20 amino acid residues. Comparison of the Drosophila gelsolin sequence with other members of the gelsolin family of actin-binding proteins reveals the characteristic segmental repeat structure found in this class of proteins. A 42% identity is observed between Drosophila secretory gelsolin and human plasma gelsolin when their primary structures are compared. Northern blots resolve a single 3000 base message in third instar Drosophila larvae, a message that appears to be encoded by a single gene located at 82A, B on the right arm of the third chromosome.
凝溶胶蛋白是一种肌动蛋白结合蛋白，具有切断和封闭肌动蛋白丝的带刺末端以及促进单体肌动蛋白组装的能力。它在脊椎动物中既被鉴定为一种细胞质蛋白，也被鉴定为一种分泌到血浆中的蛋白。在此我们报告来自果蝇的一种分泌形式的凝溶胶蛋白的全长互补DNA的核酸序列。推导的790个残基的氨基酸序列（M(r)=87,669）包含一个预测的20个氨基酸残基的信号肽。将果蝇凝溶胶蛋白序列与肌动蛋白结合蛋白凝溶胶蛋白家族的其他成员进行比较，揭示了在这类蛋白中发现的特征性片段重复结构。当比较果蝇分泌型凝溶胶蛋白和人血浆凝溶胶蛋白的一级结构时，二者有42%的同一性。Northern印迹法在三龄果蝇幼虫中分辨出一条单一的3000个碱基的信息，这条信息似乎由位于第三条染色体右臂82A、B处的一个单一基因编码。
