Protein expression in response to folate stress in Escherichia coli.
Interruption of folate metabolism by trimethoprim results in the elevated expression of folate stress proteins in Escherichia coli. E. coli grown in culture medium supplemented with the folate-dependent metabolites glycine, methionine, and the purine nucleoside inosine shows reduced expression of folate stress proteins. The folate stress proteins include the universal stress protein, the ferric uptake regulatory repressor, and possibly, lipoamide dehydrogenase, the L protein component of the glycine cleavage enzyme complex.
Huang
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Department of Chemistry, Pomona College, Claremont, California 91711, USA.
Mohler
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AM
Rohlman
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D001426:Bacterial Proteins / Q000096:biosynthesis*; D015180:Electrophoresis, Gel, Two-Dimensional; D004926:Escherichia coli / Q000187:drug effects* / Q000254:growth & development / Q000378:metabolism; D005492:Folic Acid / Q000502:physiology*; D005493:Folic Acid Antagonists / Q000494:pharmacology*; D005998:Glycine; D006360:Heat-Shock Proteins / Q000096:biosynthesis; D007288:Inosine; D007526:Isoelectric Point; D008715:Methionine; D013941:Thymine; D014295:Trimethoprim / Q000494:pharmacology*
D001426:Bacterial Proteins; D005493:Folic Acid Antagonists; D006360:Heat-Shock Proteins; C078564:universal stress protein A, Bacteria; D007288:Inosine; D005492:Folic Acid; D008715:Methionine; D014295:Trimethoprim; D013941:Thymine; D005998:Glycine