Abstract
Pyruvate formate-lyase (EC 2.3.1.54), a key enzyme in the anaerobic metabolism of Salmonella typhimurium, catalyzes the conversion of pyruvate to acetyl coenzyme A and formate. pfl::Mu dA operon fusions were isolated for the study of transcriptional regulation. pfl was transcribed both aerobically and anaerobically, but the activity increased about sixfold under anaerobic conditions. The addition of pyruvate, formate, and acetate in nutrient broth did not have any effect on the anaerobic expression of pfl. However, the addition of pyruvate to minimal glucose medium increased the anaerobic expression of pfl. The expression of pfl varied in different growth media. Anaerobic expression of pfl was lower when the culture was grown in minimal glucose medium than when it was grown in nutrient broth. When Casamino Acids (Difco Laboratories, Detroit, Mich.) were added to minimal glucose medium, the expression of pfl increased proportionally with the amount of Casamino Acids added. The transcription of pfl was positively controlled by the oxrA gene product and was affected by both the cya and crp mutations. However, mutations in genes affecting the cyclic AMP-cyclic AMP receptor protein complex or oxrA could not completely abolish the anaerobic derepression of pfl. In merodiploid strains, pfl::Mu dA/F' pfl+, the beta-galactosidase activities were decreased. The mutations gyrA, oxrC, and oxrE, which affected anaerobic metabolism, did not affect anaerobic expression of pfl.
MeSH Terms
Acetyltransferases/biosynthesis,genetics
Anaerobiosis
Bacterial Proteins/genetics
Cloning, Molecular
Enzyme Repression
Gene Expression Regulation
Genes/drug effects
Genes, Bacterial/drug effects
Genotype
Operon
Phenotype
Pyruvates/pharmacology
Salmonella typhimurium/enzymology,genetics,growth & development
Transcription, Genetic
Chemicals
Bacterial Proteins
Pyruvates
Acetyltransferases
formate C-acetyltransferase
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Wong K K
Department of Biology, Chinese University of Hong Kong, Shatin.
Suen K L
Kwan H S
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