Morikawa Kazuya, Hidaka Toshie, Murakami Hiroyuki, Hayashi Hideo, Ohta Toshiko
Institute of Basic Medical Sciences, Graduate School of Comprehensive Human Sciences, University of Tsukuba, Tennoh-dai, Tsukuba 305-8575, Japan.
FEMS Microbiol Lett. 2005 Aug 1;249(1):185-90. doi: 10.1016/j.femsle.2005.06.038.
Drp35 has been identified as a protein that is induced in Staphylococcus aureus in response to exposure to certain antibiotics. Here we demonstrate that Drp35 is a lactonase that does not contribute directly to the resistance to the inducer antibiotics except for bacitracin. The detailed analysis on the expression of Drp35 revealed that in addition to a broad range of antibiotics, agents such as detergents that perturb the membrane integrity could induce its expression. The significance of this characteristic expression is discussed in relation to its activity similarity to the eukaryotic counterparts, paraoxonase family proteins.
Drp35已被鉴定为一种蛋白质，它在金黄色葡萄球菌中因接触某些抗生素而被诱导产生。在此我们证明，Drp35是一种内酯酶，除了对杆菌肽外，它并不直接导致对诱导性抗生素产生抗性。对Drp35表达的详细分析表明，除了多种抗生素外，诸如破坏膜完整性的去污剂等物质也能诱导其表达。结合其与真核生物对应物对氧磷酶家族蛋白的活性相似性，讨论了这种特征性表达的意义。
