Synthesis of the Streptomyces lividans maltodextrin ABC transporter depends on the presence of the regulator MalR
Synthesis of the Streptomyces lividans maltodextrin ABC transporter depends on the presence of the regulator MalR
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DOI：
10.1016/s0378-1097(00)00566-8
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发表时间：
2001-03-01
影响因子：
2.1
通讯作者：
Schrempf, H
中科院分区：
文献类型：
--
作者：
Schlösser, A;Weber, A;Schrempf, H
在麦芽三糖或直链淀粉的生长过程中，变铅青链霉菌和天蓝色链霉菌A3(2)合成了对麦芽三糖具有最高专一性的麦芽糊精摄取系统。天蓝色链霉菌A3(2)突变株缺乏功能性雄性结合蛋白，其转运活性缺失。克隆和测序结果表明，天蓝色链霉菌A3(2)的操纵子与变铅青链球菌的操纵子相对应，推导出的变铅青链霉菌REG1氨基酸序列与天蓝色链霉菌A3(2)的MalR完全相同。结果表明，两株菌对麦芽糊精具有相同的ABC转运系统。在大肠杆菌中克隆了变铅青链霉菌的MalR基因，其中含有6个组氨酸编码的密码子。结果表明，纯化的6HisMalR(S1)与变铅青链球菌MalR-Male基因间隔区的两个基序结合，并在麦芽五糖存在下解离。(C)2001年欧洲微生物学会联合会。爱思唯尔科学公司出版。版权所有。
During growth with maltotriose or amylose, Streptomyces lividans and Streptomyces coelicolor A3(2) synthesize a maltodextrin uptake system with highest specificity for maltotriose. The transport activity is absent in mutants of S. coelicolor A3(2) lacking a functional MalE binding protein. Cloning and sequencing data suggest that the mal operon of S. coelicolor A3(2) corresponds to the one of S. lividans and that the deduced S. lividans Reg1 amino acid sequence is identical to that of MalR from S. coelicolor A3(2). It can be concluded that both strains have the same ABC transport system for maltodextrins. The S. lividans malR was cloned in Escherichia coli in frame with six histidine-encoding codons. The resulting, purified 6HisMalR(Sl) was shown to bind to two motifs within the S. lividans malR-malE intergenic region and to dissociate in the presence of maltopentaose. (C) 2001 Federation of European Microbiological Societies. Published by Elsevier Science B.V. All rights reserved.