Bacterial Permeases1

Cohen, Georges N.; Monod, Jacques

doi:10.1128/mmbr.21.3.169-194.1957

Cited by 324 publications

(97 citation statements)

References 1 publication

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“…Catabolite repression. The nonlinear differential rate of 5-exo-DH induction is similar to that described by Cohen et al (2,9) for induction of ,B-galactosidase in Escherichia coli using nonsaturating amounts of inducer. In those experiments the delay of a linear induction rate was due to the time required for full permease induction.…”

Section: Resultssupporting

confidence: 68%

Induction Specificity and Catabolite Repression of the Early Enzymes in Camphor Degradation by Pseudomonas putida

Hartline

Gunsalus

1971

J Bacteriol

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The ability of bornane and substituted bornanes to induce the early enzymes for D(+)-camphor degradation and control of these enzymes by catabolite repression were studied in a strain of a Pseudomonas putida. Bornane and 20 substituted bornane compounds showed induction. Of these 21 compounds, bornane and 8 of the substituted bornanes provided induction without supporting growth. Oxygen, but not nitrogen, enhanced the inductive potency of the unsubstituted bornane ring. All bornanedione isomers caused induction, and those with substituents on each of the three consecutive carbon atoms, including the methyl group at the bridgehead carbon, showed induction without supporting growth. Although it was not possible to obtain experimental data for a case of absolute gratuitous induction by compounds not supporting growth, indirect evidence in support of gratuitous induction is presented. It is proposed that the ability of P. putida to tolerate the unusually high degree of possible gratuitous induction observed for camphor catabolism may be related to the infrequent occurrence of bicyclic ring structures in nature. Survival of an organism with a broad specificity for gratuitous induction is discussed. Glucose and succinate, but not glutamate, produced catabolite repression of the early camphor-degrading enzymes. Pathway enzymes differ in their degree of sensitivity to succinate-provoked catabolite repression. The ability of a compound to produce catabolite repression is not, however, directly related to the duration of the lag period (diauxic lag) between growth on camphor and growth on the repressing compound.

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Section: Resultssupporting

confidence: 68%

Induction Specificity and Catabolite Repression of the Early Enzymes in Camphor Degradation by Pseudomonas putida

Hartline

Gunsalus

1971

J Bacteriol

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“…The kinetic studies indicate the existence of two modes of amino acid transport: one, a process concentrating amino acid in the cell in excess of the external concentration, and the other, a process in which the uptake is directly proportional to the external concentration. The first process displays saturation kinetics characteristic of enzyme function that is assumed to reflect the operation of permease which catalyzes the entry of specific substrate across a cellular osmotic barrier into the cell (5). D-Alanine uptake is mediated solely by this permease system.…”

Section: Discussionmentioning

confidence: 99%

Amino Acid Transport in Mycobacterium smegmatis

Yabu

1970

J Bacteriol

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The transport of D-alanine, D-glutamic acid, and D-valine in Mycobacterium smegmatis was compared quantitatively with that of their L-isomers. It appeared that the uptake of D-alanine was mediated by an active process displaying saturation kinetics characteristic of enzyme function, whereas the uptake of D-glutamic acid was accomplished by a passive process showing diffusion kinetics. Both processes were involved in the uptake of L-alanine, L-glutamic acid, D-valine, and L-valine. D-Valine competed with L-valine for entry into the cell through a single active process. D-Alanine and L-alanine also utilized the same active process, but the D-isomer could not enter the cell through the passive process. The passive process exhibited characteristics of diffusion, but was sensitive to sulfhydryl-blocking reagents and showed competition among structurally related amino acids. These last findings suggested that the passive process is a facilitated diffusion.

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confidence: 84%

“…The utilization of sugars, for example lactose or maltose, can take place in E8cherichia coli only in the presence of two catalytic systems, namely permease and enzymes catalysing the breakdown of the sugars within the cell (Cohen & Monod, 1957).…”

mentioning

confidence: 99%

Change in the location of amylomaltase produced by mutation in Escherichia coli

Burger¹,

Pavlasová²

1964

Biochemical Journal

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The utilization of sugars, for example lactose or maltose, can take place in E8cherichia coli only in the presence of two catalytic systems, namely permease and enzymes catalysing the breakdown of the sugars within the cell (Cohen & Monod, 1957).The present paper reports mutants that are not capable of utilizing maltose, although amylomaltase is present in the cell. The results, however, indicate that it is not crypticity to maltose that causes incapacity for utilization but a change in location that is connected with the binding of amylomaltase in the cell structure.a-Glucosidase in an inactive form bound to the cell structures of Saccharomyce8 cerevi8iae was found by Robertson & Halvorson (1957), and a similar observation was made by Axelrod (1962) in Saccharomycea oviformis. In the latter case it was shown that ribonuclease solubilizes bound aglucosidase from the cell structures.A preliminary account of this work was presented at the Third Congress of the Czechoslovak Biochemical Society, Olomouc, Czechoslovakia, 1-5 July 1963. METHODSBacterial cultures. All experiments were carried out with E. coli strain K12 from our collection numbered 3310 and with a mutant prepared from this strain denoted as 33101M.In one experiment (see Fig. 2) two further strains from our collection were used, HbL and K10-10.If not stated otherwise, cultures of the above strains were used in the early exponential phase ofgrowth, cultivated on broth [beef extract (Difoo), 0-3 %; peptone (Difco), 1% (w/v); NaCl, 1-5% (w/v); pH 7] with aeration. For the wild-type organism maltose (30 mm) was added to the medium. Growth was determined with a Pulfrich photometer at 550 mju. After growth, the bacteria were centrifuged at 00 and washed three times in O lM-phosphate buffer. The O ulM-phosphate buffer used in all experiments was prepared by adding 0l1m-Na2HPO4 to 0O1m-KH2PO4 to give a final pH of 7.For the isolation of the mutant and some other experiments, minimal medium M 63 (Pardee, Jacob & Monod, 1959) and the minimal medium described by Davis (1950), were used. These media are referred to below as minimal media.Preparation of the mutant. The mutants were obtained by essentially the same method as that used by Gorini & Kaufman (1960), with the differences that the concentration of glucose during cultivation before and after irradiation with ultraviolet light was 1% (w/v) and that sucrose was not added to the medium before subjecting the bacteria to the action of penicillin. Plating method. This was carried out to determine whether the examined strains could grow on a minimal medium, where the only carbon source was maltose. The bacteria were plated on the surface of a solid agar-medium gel, which contained minimal medium with maltose or glucose and 1-5 % (w/v) of agar (Difco). In some cases there was a soft agar layer, containing minimal medium with sugar and 0-6 % of agar (Difco) with the suspension of bacteria at 450 layered on solid agar-medium gel.Amylomaltase activity. This was determined by a modification of the method of Keston (1956...

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Bacterial Permeases1

Cited by 324 publications

References 1 publication

Induction Specificity and Catabolite Repression of the Early Enzymes in Camphor Degradation by Pseudomonas putida

Induction Specificity and Catabolite Repression of the Early Enzymes in Camphor Degradation by Pseudomonas putida

Amino Acid Transport in Mycobacterium smegmatis

Change in the location of amylomaltase produced by mutation in Escherichia coli

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