Nieto C, Espinosa M, Puyet A
Centro de Investigaciones Biológicas, Consejo Superior de Investigaciones Científicas, Velázquez 144, E-28006 Madrid, Spain.
J Biol Chem. 1997 Dec 5;272(49):30860-5. doi: 10.1074/jbc.272.49.30860.
The Streptococcus pneumoniae MalR protein regulates the transcription of two divergent operons, malXCD and malMP, involved in maltosaccharide uptake and utilization, respectively. MalR belongs to the LacI-GalR family of transcription repressors. The protein binds specifically to two operator sequences in the intergenic region between these operons. The affinity of MalR for the malMP binding sequence is higher than for the malXCD site. Results obtained in vivo using transcriptional fusions with reporter genes indicate low repression level of malXCD by MalR when compared with malMP. This behavior may be correlated with the existence of separate induction pathways for maltose, maltotriose, and maltotetraose. The similarities found at the operator sequences and binding domains for MalR and enterococcal repressor proteins suggest that the pneumococcal maltosaccharide regulation system is closely related to several Gram-negative metabolic pathways, but not to the structurally similar Escherichia coli maltose regulon.
肺炎链球菌MalR蛋白调控两个反向操纵子malXCD和malMP的转录,这两个操纵子分别参与麦芽糖的摄取和利用。MalR属于LacI-GalR转录抑制因子家族。该蛋白特异性结合这些操纵子之间基因间隔区的两个操纵序列。MalR对malMP结合序列的亲和力高于对malXCD位点的亲和力。使用与报告基因的转录融合在体内获得的结果表明,与malMP相比,MalR对malXCD的抑制水平较低。这种行为可能与麦芽糖、麦芽三糖和麦芽四糖存在单独的诱导途径有关。在MalR与肠球菌阻遏蛋白的操纵序列和结合结构域中发现的相似性表明,肺炎球菌麦芽糖调控系统与几种革兰氏阴性菌代谢途径密切相关,但与结构相似的大肠杆菌麦芽糖操纵子无关。