Trimethoprim induces heat shock proteins and protein aggregation in E. coli cells.

Ewa Laskowska, Dorota Kuczyńska-Wiśnik, Monika Bak, Barbara Lipińska

Department of Biochemistry, University of Gdańsk, Kładki 24, 80-822 Gdańsk, Poland. lasko@biotech.univ.gda.pl

Current microbiology 2003 Oct

filter terms:

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 delta ibpA/B operon resulted in increased protein aggregation but did not influence cell viability.

Citation

Ewa Laskowska, Dorota Kuczyńska-Wiśnik, Monika Bak, Barbara Lipińska. Trimethoprim induces heat shock proteins and protein aggregation in E. coli cells. Current microbiology. 2003 Oct;47(4):286-9