MacGregor, C H, Arora, S K, Hager, P W, Dail, M B, Phibbs, P V
The gene (crc) responsible for catabolite repression control in Pseudomonas aeruginosa has been cloned and sequenced. Flanking the crc gene are genes encoding orotate phosphoribosyl transferase...
Wolff, J A, MacGregor, C H, Eisenberg, R C, Phibbs, P V
Independently controlled, inducible, catabolic genes in Pseudomonas aeruginosa are subject to strong catabolite repression control by intermediates of the tricarboxylic acid cycle. Mutants which...
MacGregor, C H, Wolff, J A, Arora, S K, Phibbs, P V
Mutants which are defective in catabolite repression control (CRC) of multiple independently regulated catabolic pathways have been previously described. The mutations were mapped at 11 min on the...
Rasmussen, B A, MacGregor, C H, Ray, P H, Bassford, P J
It has not been possible to obtain in vitro expression of the positively regulated malE gene encoding the periplasmic maltose-binding protein (MBP) of Escherichia coli. To facilitate in vitro malE...
New mechanism for post-translational processing during assembly of a cytoplasmic membrane protein?
MacGregor, C H, McElhaney, G E
Insertion of nitrate reductase into the Escherichia coli cytoplasmic membrane was examined by following the fate of pulse-labeled enzyme in both the membrane and cytoplasm during various times after...
Synthesis and degradation of nitrate reductase in Escherichia coli.
The biosynthesis, insertion, and in vivo stability of nitrate reductase were examined by following the amount of labeled enzyme present in both membranes and cytoplasm at varying times after a short...
Subunits A and B were isolated from purified nitrate reductase by preparative electrophoresis in low levels of sodium dodecyl sulfate. Nonheme iron and low levels of molybdenum were associated with...
Localization of proteolytic activity in the outer membrane of Escherichia coli.
MacGregor, C H, Bishop, C W, Blech, J E
An enzyme in the cytoplasmic membrane, nitrate reductase, can be solubilized by heating membranes to 60 degrees C for 10 min at alkaline pH. A protease in the cell envelope has been shown to be...
Nitrate reductase in Escherichia coli K-12: involvement of chlC, chlE, and chlG loci.
We examined the properties of mutants of E. coli which are defective with respect to nitrate reductase activity. chlE::Mu cts and chlG::Mu cts mutants were all chlorate resistant, and the strains...
Membrane-bound nitrate reductase of Escherichia coli consists of three subunits designated as A, B, and C, with subunit C being the apoprotein of cytochrome b, A hemA mutant that cannot synthesize...
Do cytochromes function as oxygen sensors in the regulation of nitrate reductase biosynthesis?
The observation that oxygen represses nitrate reductase biosynthesis in a hemA mutant grown aerobically with or without delta-aminolevulinic acid indicates that cytochromes are not responsible for...
Solubilization of Escherichia coli nitrate reductase by a membrane-bound protease.
Nitrate reductase extracted from the membrane of Escherichia coli by alkaline heat treatment was purified to homogeneity and used to prepare specific antibody. Nitrate reductase, precipitated by this...
Anaerobic cytochrome b1 in Escherichia coli: association with and regulation of nitrate reductase.
Nitrate reductase solubilized from the membrane of Escherichia coli by alkaline heat treatment was purified to homogeneity and used to prepare specific antibody. Nitrate reductase, precipitated by...
Synthesis of nitrate reductase components in chlorate-resistant mutants of Escherichia coli.
Specific antibody to purified nitrate reductase from Escherichia coli was used to identify enzyme components present in mutants which lack functional nitrate reductase. chlA and B mutants contained...
MacGregor, C. H., Schnaitman, C. A.
Chlorate-resistant mutants corresponding to each known genetic locus (chlA, chlB, chlC, chlD, chlE) were isolated from Escherichia coli K-12. All these mutants showed decreased amounts of...
MacGregor, C. H., Schnaitman, C. A.
The reconstitution of nitrate reductase activity in mixtures of cytoplasmic fractions from the chlorate-resistant mutants chlA, B, C, and E which are lacking this activity was investigated, and the...
MacGregor, C H, Arora, S K, Hager, P W, Dail, M B, Phibbs, P V
The gene (crc) responsible for catabolite repression control in Pseudomonas aeruginosa has been cloned and sequenced. Flanking the crc gene are genes encoding orotate phosphoribosyl transferase...
Wolff, J A, MacGregor, C H, Eisenberg, R C, Phibbs, P V
Independently controlled, inducible, catabolic genes in Pseudomonas aeruginosa are subject to strong catabolite repression control by intermediates of the tricarboxylic acid cycle. Mutants which...
MacGregor, C H, Wolff, J A, Arora, S K, Phibbs, P V
Mutants which are defective in catabolite repression control (CRC) of multiple independently regulated catabolic pathways have been previously described. The mutations were mapped at 11 min on the...
Rasmussen, B A, MacGregor, C H, Ray, P H, Bassford, P J
It has not been possible to obtain in vitro expression of the positively regulated malE gene encoding the periplasmic maltose-binding protein (MBP) of Escherichia coli. To facilitate in vitro malE...
New mechanism for post-translational processing during assembly of a cytoplasmic membrane protein?
MacGregor, C H, McElhaney, G E
Insertion of nitrate reductase into the Escherichia coli cytoplasmic membrane was examined by following the fate of pulse-labeled enzyme in both the membrane and cytoplasm during various times after...
Synthesis and degradation of nitrate reductase in Escherichia coli.
The biosynthesis, insertion, and in vivo stability of nitrate reductase were examined by following the amount of labeled enzyme present in both membranes and cytoplasm at varying times after a short...
Subunits A and B were isolated from purified nitrate reductase by preparative electrophoresis in low levels of sodium dodecyl sulfate. Nonheme iron and low levels of molybdenum were associated with...
Localization of proteolytic activity in the outer membrane of Escherichia coli.
MacGregor, C H, Bishop, C W, Blech, J E
An enzyme in the cytoplasmic membrane, nitrate reductase, can be solubilized by heating membranes to 60 degrees C for 10 min at alkaline pH. A protease in the cell envelope has been shown to be...
Nitrate reductase in Escherichia coli K-12: involvement of chlC, chlE, and chlG loci.
We examined the properties of mutants of E. coli which are defective with respect to nitrate reductase activity. chlE::Mu cts and chlG::Mu cts mutants were all chlorate resistant, and the strains...
Membrane-bound nitrate reductase of Escherichia coli consists of three subunits designated as A, B, and C, with subunit C being the apoprotein of cytochrome b, A hemA mutant that cannot synthesize...
Do cytochromes function as oxygen sensors in the regulation of nitrate reductase biosynthesis?
The observation that oxygen represses nitrate reductase biosynthesis in a hemA mutant grown aerobically with or without delta-aminolevulinic acid indicates that cytochromes are not responsible for...
Solubilization of Escherichia coli nitrate reductase by a membrane-bound protease.
Nitrate reductase extracted from the membrane of Escherichia coli by alkaline heat treatment was purified to homogeneity and used to prepare specific antibody. Nitrate reductase, precipitated by this...
Anaerobic cytochrome b1 in Escherichia coli: association with and regulation of nitrate reductase.
Nitrate reductase solubilized from the membrane of Escherichia coli by alkaline heat treatment was purified to homogeneity and used to prepare specific antibody. Nitrate reductase, precipitated by...
Synthesis of nitrate reductase components in chlorate-resistant mutants of Escherichia coli.
Specific antibody to purified nitrate reductase from Escherichia coli was used to identify enzyme components present in mutants which lack functional nitrate reductase. chlA and B mutants contained...
MacGregor, C. H., Schnaitman, C. A.
Chlorate-resistant mutants corresponding to each known genetic locus (chlA, chlB, chlC, chlD, chlE) were isolated from Escherichia coli K-12. All these mutants showed decreased amounts of...
MacGregor, C. H., Schnaitman, C. A.
The reconstitution of nitrate reductase activity in mixtures of cytoplasmic fractions from the chlorate-resistant mutants chlA, B, C, and E which are lacking this activity was investigated, and the...