Gouin E, Dehoux P, Mengaud J, Kocks C, Cossart P
Unité des Interactions Bactéries-Cellules, Institut Pasteur, Paris, France.
Infect Immun. 1995 Jul;63(7):2729-37. doi: 10.1128/iai.63.7.2729-2737.1995.
A gene homologous to the actA gene of Listeria monocytogenes was cloned from Listeria ivanovii (strain CLIP257) by chromosome walking starting from the ilo gene that encodes the pore-forming toxin ivanolysin. The nucleotide sequence revealed that this gene, named iactA, encodes a protein of 1,044 amino acids (IactA) comprising a central region with seven highly conserved tandem proline-rich repeats of 47 amino acids. Although IactA and ActA share an overall similar structure, these two proteins are only distantly related. Like ActA, IactA migrates aberrantly on sodium dodecyl sulfate gels. When expressed in an L. monocytogenes actA deletion mutant strain, iactA restored actin polymerization.
通过染色体步移技术,从编码成孔毒素伊氏溶素的ilo基因开始,从伊氏李斯特菌(菌株CLIP257)中克隆出了一个与单核细胞增生李斯特菌actA基因同源的基因。核苷酸序列显示,这个名为iactA的基因编码一种由1044个氨基酸组成的蛋白质(IactA),该蛋白质包含一个中心区域,有七个高度保守的47个氨基酸的富含脯氨酸的串联重复序列。虽然IactA和ActA总体结构相似,但这两种蛋白质的亲缘关系较远。与ActA一样,IactA在十二烷基硫酸钠凝胶上迁移异常。当在单核细胞增生李斯特菌actA缺失突变株中表达时,iactA恢复了肌动蛋白聚合。