Evidence for induced synthesis of an active transport factor for mandelate in <i>Pseudomonas putida</i>

Higgins, S. J.; Mandelstam, J.

doi:10.1042/bj1260917

Cited by 21 publications

(12 citation statements)

References 17 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The mechanism of benzoate uptake is not sufficiently defined, although ample evidence has been presented for proton motive force (Ap)-driven rather than ATP-driven uptake (17,18). The uptake of mandelate by P. putida has also been studied (7,8). According to Hegeman (7), mandelate enters the cell by passive diffusion.…”

mentioning

confidence: 99%

Energy-dependent uptake of 4-chlorobenzoate in the coryneform bacterium NTB-1

et al. 1990

View full text Add to dashboard Cite

The uptake of 4-chlorobenzoate (4-CBA) in intact cells of the coryneform bacterium NTB-1 was investigated. Uptake and metabolism of 4-CBA were observed in cells grown in 4-CBA but not in glucose-grown cells. Under aerobic conditions, uptake of 4-CBA occurred with a high apparent affinity (apparent Kt, 1.7 microM) and a maximal velocity (Vmax) of 5.1 nmol min-1 mg of protein-1. At pH values below 7, the rate of 4-CBA uptake was greatly reduced by nigericin, an ionophore which dissipates the pH gradient across the membrane (delta pH). At higher pH values, inhibition was observed only with valinomycin, an ionophore which collapses the electrical potential across the membrane (delta psi). Under anaerobic conditions, no uptake of 4-CBA was observed unless an alternative electron acceptor was present. With nitrate as the terminal electron acceptor, 4-CBA was rapidly accumulated by the cells to a steady-state level, at which uptake of 4-CBA was balanced by excretion of 4-hydroxybenzoate. The mechanism of energy coupling to 4-CBA transport under anaerobic conditions was further examined by the imposition of an artificial delta psi, delta pH, or both. Uptake of 4-CBA was shown to be coupled to the proton motive force, suggesting a proton symport mechanism. Competition studies with various substrate analogs revealed a very narrow specificity of the 4-CBA uptake system. This is the first report of carrier-mediated transport of halogenated aromatic compounds in bacteria.

show abstract

mentioning

confidence: 99%

Energy-dependent uptake of 4-chlorobenzoate in the coryneform bacterium NTB-1

et al. 1990

View full text Add to dashboard Cite

show abstract

“…Cells that were heated that specific carriers for this class of compounds need not for 5 min failed to accumulate label, indicating that necessarily be evoked (18). However, the existence of trans-;ybenzoate was not simply sticking to the surfaces of porters for several aromatic acids, including 4-chlorobenzoate, addition, labeled 4-hydroxybenzoate, extracted from 4-hydroxybenzoate, and mandelate, has been inferred from lls and analyzed by thin-layer chromatography, was physiological studies (2,14,23). In addition, at least three ) be unmodified, confirming that E. coli did not groups have described aromatic acid permease mutants.…”

mentioning

confidence: 99%

Identification of the pcaRKF gene cluster from Pseudomonas putida: involvement in chemotaxis, biodegradation, and transport of 4-hydroxybenzoate

et al. 1994

View full text Add to dashboard Cite

Aromatic compounds are abundant in the biosphere as components of the complex polymer lignin and as environmental pollutants. The bacterial biodegradation of structurally simple, readily degradable aromatic compounds has been studied with the expectation that this will facilitate work on more recalcitrant members of the group. As a result, much information has been obtained about the enzymology and molecular regulation of aerobic pathways of aromatic compound degradation (6,16,35,53). An aspect of aromatic biology that has received almost no attention, however, is the question of how bacteria sense and respond to the presence of aromatic compounds in their environment. Chemotaxis and transport are two physiological functions that operate in this capacity, and a number of studies have shown that aromatic acids such as benzoate and 4-hydroxybenzoate are strong chemoattractants for Pseudomonas putida, as well as a number of other species of gram-negative bacteria including Agrobacterium spp. and rhizobia (19,20,31,39,40). However, very little is known about the characteristics of the presumed receptor proteins that are responsible for initial attractant recognition. Similarly, although a number of studies have inferred the existence of specific transport systems for aromatic acids and related compounds, only a few detailed studies of aromatic compound permeases have been reported (1, 2, 14, 30), and no molecular analyses of bacterial genes that encode such proteins have been presented.

show abstract

“…ADP1 [9]), 4-HBa (Klebsiella pneumoniae [5], Acinetobacter sp. [2]), Klebsiella planticola [3], P. putida [12]), protocatechuate (P. putida [28]), mandelate (P. putida [17]), phenylacetate (P. putida [33]), 4-hydroxyphenylacetate (Escherichia coli [31], K. pneumoniae [4]), and phthalate and 4-methylphthalate (Burkholderia fungorum [8,32]). Chlorinated aromatic compounds for which transporters have been demonstrated are 4-chlorobenzoate (coryneform bacterium strain NTB-1 [10]), 2,4-dichlorophenoxyacetate (Ralstonia eutropha [24], Sphingomonas herbicidovorans [38]), and dichlorprop (S. herbicidovorans [38]).…”

mentioning

confidence: 99%

Transporter-MediatedUptake of 2-Chloro- and 2-Hydroxybenzoate by Pseudomonashuttiensis StrainD1

Yuroff

Sabat

Hickey

2003

Appl Environ Microbiol

View full text Add to dashboard Cite

We investigated the mechanisms of uptake of 2-chlorobenzoate (2-CBa) and 2-hydroxybenzoate (2-HBa) by Pseudomonas huttiensis strain D1. Uptake was monitored by assaying intracellular accumulation of 2-[UL-ring-14 C]CBa and 2-[UL-ring-14 C]HBa. Uptake of 2-CBa showed substrate saturation kinetics with an apparent K m of 12.7 ؎ 2.6 M and a maximum velocity (V max ) of 9.76 ؎ 0.78 nmol min ؊1 mg of protein ؊1 . Enhanced rates of uptake were induced by growth on 2-CBa and 2-HBa, but not by growth on benzoate or 2,5-di-CBa. Intracellular accumulations of 2-CBa and 2-HBa were 109-and 42-fold greater, respectively, than the extracellular concentrations of these substrates and were indicative of uptake mediated by a transporter rather than driven by substrate catabolism ("metabolic drag"). Results of competitor screening tests indicated that the substrate range of the transporter did not include other o-halobenzoates that serve as growth substrates for strain D1 and for which the metabolism was initiated by the same dioxygenase as 2-CBa and 2-HBa. This suggested that multiple mechanisms for substrate uptake were coupled to the same catabolic enzyme. The preponderance of evidence from tests with metabolic inhibitors and artificial electrochemical gradients suggested that 2-CBa uptake was driven by ATP hydrolysis. If so, the 2-CBa transporter would be the first of the ATP binding cassette type implicated in uptake of haloaromatic acids.

show abstract

Evidence for induced synthesis of an active transport factor for mandelate in Pseudomonas putida

Cited by 21 publications

References 17 publications

Energy-dependent uptake of 4-chlorobenzoate in the coryneform bacterium NTB-1

Energy-dependent uptake of 4-chlorobenzoate in the coryneform bacterium NTB-1

Identification of the pcaRKF gene cluster from Pseudomonas putida: involvement in chemotaxis, biodegradation, and transport of 4-hydroxybenzoate

Transporter-MediatedUptake of 2-Chloro- and 2-Hydroxybenzoate by Pseudomonashuttiensis StrainD1

Contact Info

Product

Resources

About