Observations on Methionine Transport in Pseudomonas fluorescens UK1

Mäntsälä, Pekka; Laakso, Simo; Nurmikko, Veikko

doi:10.1099/00221287-84-1-19

Cited by 12 publications

(4 citation statements)

References 21 publications

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“…Little was known about the mechanism of transport of methionine sulfoxide in bacteria, except that sulfoxide was a poor inhibitor of methionine transport (1,12,14). Starting from the observation that methionine sulfoxide supported the growth of methionine auxotrophs in Salmonella typhimurium, I investigated whether the sulfoxide was transported by one of the methionine transport systems or whether it entered the cell by a different route.…”

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confidence: 99%

Methionine sulfoxide is transported by high-affinity methionine and glutamine transport systems in Salmonella typhimurium

Ayling¹

1981

J Bacteriol

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Three lines of evidence indicated that methionine sulfoxide is transported by the high-affinity methionine and glutamine transport systems in Salmonella typhimurium. First, methionine-requiring strains (metE) which have mutations affecting both of these transport systems (metP glnP) were unable to use methionine sulfoxide as a source of methionine. These strains could still grow on L-methionine because they possessed a low-affinity system (or systems) which transported L-methionine but not the sulfoxide. A methionine auxotroph with a defect only in the metP system, which was dependent upon the glnP+ system for the transport of methionine sulfoxide, was inhibited by L-glutamine because glutamine inhibited the transport of the sulfoxide by the glnP+ system. Second, a metE metP glnP strain could be transduced at either the metP or glnP genes to restore its ability to grow on methionine sulfoxide. Third, the transport of [14C]methionine sulfoxide was inhibited by methionine and by glutamine in the metP+ glnP+ strain. No transport was detected in the metP glnP double-mutant strain.

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Methionine sulfoxide is transported by high-affinity methionine and glutamine transport systems in Salmonella typhimurium

Ayling¹

1981

J Bacteriol

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“…B. linens CNRZ 918, like Pseudomonas fluorescens UK1 (20,23), has only one L-methionine transport system with low affinity (Km = 55 ,uM). In contrast, the existence of two systems with high and low affinities has been shown in E. coli (14, 17) and S. typhimurium (1, 2).…”

Section: Discussionmentioning

confidence: 99%

Na ⁺ -Stimulated Transport of l -Methionine in Brevibacterium linens CNRZ 918

Ferchichi

Hemme

Nardi

1987

Appl Environ Microbiol

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The transport of L-methionine by the gram-positive species Brevibacterium linens CNRZ 918 is described. The one transport system (Km = 55 ,uM) found is constitutive for L-methionine, stereospecific, and pH and temperature dependent. Entry of L-methionine into cells is controlled by the internal methionine pool. Competition studies indicate that L-methionine and aL-aminobutyric acid share a common carrier for their transport. Neither methionine derivatives substituted on the amino or carboxyl groups nor D-methionine was an inhibitor, whereas powerful inhibition was shown by L-cysteine, s-methyl-L-cysteine, DL-selenomethionine and DL-homocysteine. Sodium plays important and varied roles in L-methionine transport by B. linens CNRZ 918: (i) it stimulates transport without affecting the Km, (ii) it increases the specific activity (on a biomass basis) of the L-methionine transport system when present with methionine in the medium, suggesting a coinduction mechanism. L-Methionine transport requires an exogenous energy source, which may be succinic, lactic, acetic, or pyruvic acid but not glucose or sucrose. The fact that L-methionine transport was stimulated by potassium arsenate and to a lesser extent by potassium fluoride suggests that high-energy phosphorylated intermediates are not involved in the process. Monensin eliminates stimulation by sodium. Gramicidin and carbonyl cyanide-m-chlorophenylhydrazone act in the presence or absence of Na+. N-Ethylmaleimide, p-chloromercurobenzoate, valinomycin, sodium azide, and potassium cyanide have no or only a partial inhibitory effect. These results tend to indicate that the proton motive force reinforced by the Na+ gradient is involved in the mechanism of energy coupling of L-methionine transport by B. linens CNRZ 918. Thus, this transport is partially similar to the well-described systems in gram-negative bacteria, except for the role of sodium, which is very effective in B. linens, a species adapted to the high sodium levels of its niche.

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“…fluorescens UKI has an inducible methionine transport system with a Km of 25 j.LM (Mantsala et al, 1974) which has broad specificity for amino acids (Laakso, 1976). Membrane vesicles prepared from methionine-grown P. fluorescens UKI exhibit methionine uptake in an energydependent manner, suggesting that the transport system is a carriermediated transport system (Mantsala et al, 1974). P. aeruginosa also has a high-affinity, energy-requiring methionine transport system with a Km of 0.2-0.3 j.LM .…”

Section: Methioninementioning

confidence: 99%

Pseudomonas

1998

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Observations on Methionine Transport in Pseudomonas fluorescens UK1

Cited by 12 publications

References 21 publications

Methionine sulfoxide is transported by high-affinity methionine and glutamine transport systems in Salmonella typhimurium

Methionine sulfoxide is transported by high-affinity methionine and glutamine transport systems in Salmonella typhimurium

Na ⁺ -Stimulated Transport of l -Methionine in Brevibacterium linens CNRZ 918

Pseudomonas

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Observations on Methionine Transport in Pseudomonas fluorescens UK1

Cited by 12 publications

References 21 publications

Methionine sulfoxide is transported by high-affinity methionine and glutamine transport systems in Salmonella typhimurium

Methionine sulfoxide is transported by high-affinity methionine and glutamine transport systems in Salmonella typhimurium

Na + -Stimulated Transport of l -Methionine in Brevibacterium linens CNRZ 918

Pseudomonas

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Na ⁺ -Stimulated Transport of l -Methionine in Brevibacterium linens CNRZ 918