The Control of Sulphate Activation in Bacteria

Wheldrake, J.F.; Pasternak, C. A.

doi:10.1042/bj0960276

Cited by 37 publications

(19 citation statements)

References 14 publications

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“…Repression and end product inhibition of the enzymes concerned with sulfate reduction is also well established in microorganisms (9,17,25 The interactions of amino acids with L-cyst(e)ine and L-isoleucine in sulfate uptake are reminiscent of interactions reported in other systems. In general, amino acid transport involves competition within groups of amino acids for uptake sites in bacteria (4), fungi (5) and animal cells ' (16).…”

Section: Discussionmentioning

confidence: 89%

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Regulation of Sulfate Uptake by Amino Acids in Cultured Tobacco Cells

Hart

Filner

1969

Plant Physiol.

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Abstract. The sulfur requirements of tobacco (Nicotiana tabacum L. var. Xanthi) XD cells grown in chemically defined liquid media can be satisfied by sulfate, thiosulfate, L-cyst(e)ine, L-methionine or glutathione, and somewhat less effectively by D-cyst(e)ine, D-methionine or DL-homocyst(e)ine. SuHfate uptake is inhibited after a 2 hr log by L-cyst(e)ine, L-methionine, L-homocyst(e)ine or L-isoleucine, but not by any of the other protein amino acids, nor by D-cyst(e)ine. L-cyst(e)ine is neither a competitive nor a non-oompetitive inhibitor of sulfate uptake. Its action most closely resembles apparent uncompetitive inhibition.. Inhibition of sulfate uptake by L-cyst(e)ine can be partially prevented by equimolar L-arginine, L-lysine, L-leucine, L-phenylalanine, L-tyrosine or L-tryptophan, but is little affeoted by any of the other protein amino acids. The effective amino acids are apparent competitive inhibitors of L-cyst(e)ine uptake after a 2 hr lag. Inhibition of sulfate uptake by L-methionine cannot be prevented, nor can uptake of L-methionine be inhibited by any single protein amino acid. The results suggest the occurrence of negative feedback control of sulfate assimilation by the end products, the sulfur amino acids, in cultured tobacco cells.

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Section: Discussionmentioning

confidence: 89%

“…The sulfate transport system is repressed by cysteine in Salmonella typhimurium (6). The sulfate reducing enzymes are repressible in several species of bacteria (7,17,25), the apparent corepressor again being cysteine (9,24).…”

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confidence: 99%

Regulation of Sulfate Uptake by Amino Acids in Cultured Tobacco Cells

Hart

Filner

1969

Plant Physiol.

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“…ATP-sulfurylase was also found in roots of corn seedlings grown aseptically. The data suggest that at least the first reaction in sulfate reduction might proceed as effectively in roots as in shoots.The mechanisms of sulfate reduction in microorganisms have been studied extensively (10,14,15,17,(23)(24)(25). These studies showed that the first step in the metabolism of sulfate is the activation of sulfate by ATP-sulfurylase (EC 2.7.7.4) according to the following: ATP + SO42= APS + PPi…”

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confidence: 99%

Adenosine 5′-Triphosphate-Sulfurylase in Corn Roots and Its Partial Purification

Onajobi

Cole²,

Ross³

1973

Plant Physiol.

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ATP-sulfurylase (ATP-sulfate adenyltransferase, EC 2.7.7.4) was found in nonparticulate fractions of both roots and leaves of Zea mays L. seedlings using two detection methods. Addition of exogenous pyrophosphatase was essential for maximum rates of conversion of 3SO2-to labeled adenosine phosphosulfate in unpurified root extracts, but not in unpurified leaf extracts. In the presence of exogenous pyrophosphatase, the enzyme from roots exhibited specific activities as high as those obtained with the leaf enzyme. The root enzyme was purified 33-fold by centrifugation and column chromatography procedures. Its molecular weight obtained by Sephadex gel filtration was about 42,000. Its Kit for pyrophosphate was 7 AM, while for adenosine phosphosulfate, the Km was 1.35 uM.None of the enzyme fractions studied converted adenosine phosphosulfate into detectable amounts of 3'-phosphoadenosine-5'-phosphosulfate. ATP-sulfurylase was also found in roots of corn seedlings grown aseptically. The data suggest that at least the first reaction in sulfate reduction might proceed as effectively in roots as in shoots.The mechanisms of sulfate reduction in microorganisms have been studied extensively (10,14,15,17,(23)(24)(25). These studies showed that the first step in the metabolism of sulfate is the activation of sulfate by ATP-sulfurylase (EC 2.7.7.4) according to the following: ATP + SO42= APS + PPiIn some microorganisms, an enzyme APS3-kinase (EC 2.7.1.25) further activates APS to PAPS (8,15 Most studies of sulfate reduction in higher plants have been limited to leaves. However, Ellis (7) and Balharry and Nicholas (4) demonstrated substantial ATP-sulfurylase activities in tomato roots and root tips of oat seedlings, respectively. We have discovered that excised corn roots show as much ATP-sulfurylase activity as corn leaves. This paper presents a method for partial purification and some properties of the ATP-sulfurylase of corn roots. MATERIALS AND METHODSRadioactive materials (H2I'SO, and H332P04) were obtained The roots of these seedlings were freed of agar and used for the preparation of sulfurylase enzyme under sterile conditions.

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“…In Escherichia coli the synthesis of the enzymes catalysing the reduction of sulphate to sulphide is repressed by cysteine (Mager, 1960;Pasternak, 1961Pasternak, , 1962Kemp, Atkinson, Ehret & Lazzarini, 1963;Ellis, Humphries & Pasternak, 1964;Pasternak, Ellis, Jones-Mortimer & Crichton, 1965;Wheldrake & Pasternak, 1965). Pasternak et al (1965), who showed that the sulphate-reducing enzymes are not all repressed in a co-ordinate manner, suggested that a mechanism of 'differential repression' might operate.…”

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confidence: 99%

Intracellular concentration of cysteine in Escherichia coli and its relation to repression of the sulphate-activating enzymes

Wheldrake

1967

Biochemical Journal

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1. The intracellular cysteine and glutathione concentrations were measured in Escherichia coli under a variety of growth conditions. 2. An inverse relation between intracellular cysteine concentration and the specific activity of the sulphate-activating enzymes was found. 3. This is compatible with the view that the intracellular cysteine concentration controls the rate of synthesis of these enzymes.

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The Control of Sulphate Activation in Bacteria

Cited by 37 publications

References 14 publications

Regulation of Sulfate Uptake by Amino Acids in Cultured Tobacco Cells

Regulation of Sulfate Uptake by Amino Acids in Cultured Tobacco Cells

Adenosine 5′-Triphosphate-Sulfurylase in Corn Roots and Its Partial Purification

Intracellular concentration of cysteine in Escherichia coli and its relation to repression of the sulphate-activating enzymes

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