中文摘要：

盘基网柄菌Dictyostelium discoideum是目前黏菌中研究最清楚的模式生物，其捕食过程与肌动蛋白的多聚化密切相关。为探讨盘基网柄菌肌动蛋白的序列特征，本研究利用生物信息学方法分析了盘基网柄菌32条肌动蛋白的蛋白一蛋白相互作用（protein．protein interaction）和可能含有的保守基序。结果表明：盘基网柄菌32条肌动蛋白与其他蛋白存在一组复杂相互作用关系和5组比较简单的相互作用关系；利用MEMESUITE分别分析盘基网柄菌32条肌动蛋白序列的保守基序和与actinl7呈最佳匹配的21种生物肌动蛋白的保守基序，结果共获得6个保守基序，即motifl，motif2，motif3，Motifl，Motif2，Motif3。其中motifl，Motifl，Motif3为本研究新发现的保守基序，这3个保守基序可定位于Profilin-actin．VASP202_244（PDBID：3CHW）三维结构的重要位置。以上结果表明actin3，actinlO，actinl4，actinl5，actinl7，actin31可能为盘基网柄菌比较重要的肌动蛋白；motifl，Motifl，Motif3可能是盘基网柄菌肌动蛋白在进化中重要的保守基序。

英文摘要：

Dictyostelium discoideum is widely used as a model organism in slime mold. Its predation process is closely related to actins polymerization. To investigate the characteristics of actins from D. discoideum, the protein-protein interaction （PPI） and conserved motifs of 32 actins from D. discoideum were analyzed by bioinformatics analysis. The results indicated that there is a set of complex interactions and five groups of simple interactions within the 32 actins and other proteins. By using MEME SUITE analysis method, conserved motifs of 32 actin sequences and those of 21 actin sequences of other organisms, optimally matching with actin17 were analysed. As a result, six conserved motifs motif1, motif2, motif3, Motif1, Motif2, and Motif3 wereobtained. Of which three motifs, motif1, Motif1 and structure of profiling-actin-VASP202-244. All these resu mportant actin for D. discoideum, and motif1, Motif1 Motif3 ts sugg and M , were newly found in this study, which were located on the crystal ested that actin3, actinl0, actin14, actin15, actin17, actin31 may be otif3 may play important role in the evolution of conserved motifs.