Abstract
The fumarate reductase (frdABCD), dimethyl sulfoxide (DMSO)-trimethylamine-N-oxide (TMAO) reductase (dmsABC), and nitrate reductase (narGHJI) operons in Escherichia coli encode enzymes involved in anaerobic respiration to the electron acceptors fumarate, DMSO or TMAO, and nitrate, respectively. They are regulated in response to anaerobiosis and nitrate availability. To determine how each operon is regulated in response to changes in cell growth rate and in oxygen availability, expression of frdA-lacZ, dmsA-lacZ, and narG-lacZ fusion genes was examined during continuous culture. After a change in the cell growth rate, each anaerobic electron transport pathway operon fusion responded somewhat differently. Whereas frdA-lacZ expression increased by fivefold as the growth rate decreased from 0.60 to 0.12/hour during aerobic growth, little change was seen under anaerobic conditions. In contrast, growth rate-dependent expression of narG-lacZ expression occurred under anaerobic conditions but not under aerobic conditions. Finally, dmsA-lacZ expression did not vary greatly for any of the growth rates tested. When cells were shifted from aerobic to anaerobic growth conditions, expression of each fusion increased at a moderate rate and peaked or "overshot" before reaching a new equilibrium value. This "overshoot" phenomenon was independent of the fnr gene product, which functions as a transcriptional activator of each respiratory operon during anaerobic conditions. In contrast to the moderate rate of anaerobic induction seen for narG-lacZ expression, the addition of nitrate caused a rapid induction response. The cell appears to have many ways to adjust cell respiration in response to changes in cell growth conditions.
MeSH Terms
Aerobiosis
Anaerobiosis
Cell Division
Electron Transport/genetics
Escherichia coli/genetics,growth & development,metabolism
Gene Expression Regulation, Bacterial/drug effects
Genes, Reporter
Iron-Sulfur Proteins
Lac Operon
Nitrates/pharmacology
Nitrite Reductases/biosynthesis,genetics
Operon/genetics
Oxidoreductases/biosynthesis,genetics
Oxidoreductases, N-Demethylating/biosynthesis,genetics
Oxygen/pharmacology
Recombinant Fusion Proteins/biosynthesis
Succinate Dehydrogenase/biosynthesis,genetics
Chemicals
Iron-Sulfur Proteins
Nitrates
Recombinant Fusion Proteins
Oxidoreductases
Succinate Dehydrogenase
Oxidoreductases, N-Demethylating
trimethylamine dehydrogenase
Nitrite Reductases
dimethyl sulfoxide reductase
Oxygen
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Tseng C P
Department of Microbiology and Molecular Genetics, University of California, Los Angeles 90024.
Hansen A K
Cotter P
Gunsalus R P
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