Bresnick A R, Warren V, Condeelis J
Department of Anatomy and Structural Biology, Albert Einstein College of Medicine, Bronx, New York 10461.
J Biol Chem. 1990 Jun 5;265(16):9236-40.
Tryptic digestion of ABP-120, an actin cross-linking protein from Dictyostelium discoideum, generates a ladder of peptides differing in molecular mass by 13,000 daltons, indicating a structural repeat within the molecule. A number of peptides bind actin with the smallest having a molecular mass of 17,000 daltons (T17). Our sedimentation assays also show that a peptide of 14,000 daltons does not bind actin. Using the full-length cDNA sequence (Noegel, A., Rapp, S., Lottspeich, F., Schleicher, M., and Stewart, M. (1989) J. Cell Biol. 109, 607-618) and protein sequencing techniques, we have determined that T17 begins at residue 89 while T14 begins at residue 116. Therefore we have localized 27 amino acids which are essential for actin binding activity. This region is at the end of the molecule, distal from the repetitive beta-sheet region predicted from the cDNA sequence, and displays high sequence identity with regions in the N termini of ABP/filamin, dystrophin, beta-spectrin, and alpha-actinin.
对来自盘基网柄菌的肌动蛋白交联蛋白ABP-120进行胰蛋白酶消化，会产生一系列分子量相差13,000道尔顿的肽段，这表明该分子内存在结构重复。许多肽段能与肌动蛋白结合，其中最小的肽段分子量为17,000道尔顿（T17）。我们的沉降分析还表明，一个14,000道尔顿的肽段不与肌动蛋白结合。利用全长cDNA序列（Noegel, A., Rapp, S., Lottspeich, F., Schleicher, M., and Stewart, M. (1989) J. Cell Biol. 109, 607 - 618）和蛋白质测序技术，我们确定T17从第89位氨基酸残基开始，而T14从第116位氨基酸残基开始。因此，我们定位了27个对肌动蛋白结合活性至关重要的氨基酸。该区域位于分子末端，远离根据cDNA序列预测的重复β折叠区域，并且与ABP/细丝蛋白、肌营养不良蛋白、β-血影蛋白和α-辅肌动蛋白N端区域具有高度序列同一性。
