Trimethoprim induces heat shock proteins and protein aggregation in E-coli cells
Trimethoprim induces heat shock proteins and protein aggregation in E-coli cells
复制标题
DOI：
10.1007/s00284-002-4007-z
复制
发表时间：
2003-10-01
影响因子：
2.6
通讯作者：
Lipinska, B
中科院分区：
文献类型：
--
作者：
Laskowska, E;Kuczynska-Wisnik, D;Lipinska, B
甲氧苄氨嘧啶（TMP）是二氢叶酸还原酶的抑制剂，可降低四氢叶酸的水平，为核苷酸、蛋白质和泛酸的生物合成提供一个碳单元。我们首次证明了TMP在大肠杆菌中的作用之一。大肠杆菌细胞的主要作用是蛋白质聚集和热休克蛋白（Hsps）的诱导。TMP诱导DnaK、DnaJ、GroEL、Clp B和IbpA/B Hsps。在这些Hsps中，IbpA/B被TMP最有效地诱导并与不溶性蛋白共聚集。在叶酸胁迫下，DeltaibpA/B操纵子的缺失导致蛋白质聚集增加，但不影响细胞活力。
Trimethoprim (TMP), an inhibitor of dihydrofolate reductase, decreases the level of tetrahydrofolate supplying one-carbon units for biosynthesis of nucleotides, proteins, and panthotenate. We have demonstrated for the first time that one of the effects of the TMP action in E. coli cells is protein aggregation and induction of heat shock proteins (Hsps). TMP caused induction of DnaK, DnaJ, GroEL, ClpB, and IbpA/B Hsps. Among these Hsps, IbpA/B were most efficiently induced by TMP and coaggregated with the insoluble proteins. Upon folate stress, deletion of the DeltaibpA/B operon resulted in increased protein aggregation but did not influence cell viability.