Activation of l-methionine and l-ethionine by pH 5 fraction of rat liver

Glenn, Joseph L.

doi:10.1016/0003-9861(61)90102-3

Cited by 24 publications

(7 citation statements)

References 10 publications

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“…Of the methionine analogues tested, i.e. the sulphone, sulphoxide, sulphoximine, and homocystine and ethionine, only the latter was active (Berg, 1956; Lewis, 1963; Moustafa, 1964) with a K , of approximately 3 x I O -~M (Glenn, 1961). Although not further substantiated, Rendi et al (1958) have reported L-ethionine to be inactive, while Glenn (1961) has reported D-methionine to be slightly active.…”

Section: ( E ) Sulphur Amino Acidsmentioning

confidence: 98%

“…Aminoacyl-s-RNA synthetases have been isolated from rat liver (Hele, 1961 ;Glenn, 1961;Fraser, 1963;Fraser & Klass, 1963;Boyko & Fraser, 1964), pig liver (Hele & Finch, 1960;Webster, 1961 b), guinea-pig liver (Ogata et al 1961) and from hog pancreas (Schweet, 1957). These enzymes have also been reported from chick embryo (Coronado, Mardones & Allende, 1963 ;Bublitz, 1966), from rat mammary gland (Bucovaz & Davis, 1961), from mouse and human skeletal muscle (Pennington, 1960), from frog and tadpole liver (DeGroot & Cohen, 1962), from pig thyroid (Alexander, 1963), from the small intestinal epithelium of hamsters, rats and guinea-pigs (Kessler, Eisler & Janowitz, 1965) and from four classes of Chordata (Glebov, Zaitseva & Belozerskii, 1965).…”

Section: (I) Species Occurrencesmentioning

confidence: 99%

“…Aminoacyl-s-RNA synthetases specific for cysteine have been largely neglected for both substrate specificity studies and in purification programmes. This enzyme has been detected in low concentrations in wheat germ (Moustafa & Lyttleton, (Lewis, 1963), rat liver (Rendi, Di Milia & Fronticelli, 1958; Glenn, 1961) and from wheat germ (Moustafa, 1964).…”

Section: ( E ) Sulphur Amino Acidsmentioning

confidence: 99%

“…In addition to using purified enzyme, Makman & Cantoni (1965) and Calendar & Berg (1966b) There is a much closer relationship between the various K, values measured by hydroxamate formation with different amino acids than with the other two assay methods. For example, the aminoacyl-s-RNA synthetase for methionine from rat liver, for serine from beef pancreas, and phenylalanine from E. coli are 5 x IO-*, 6 x 10-* and 4.4 x IO+ respectively (Glenn, 1961 ; , 1 9 6 4~) .…”

Section: Additional Properties Of Aminoacyl-s-rna Synthetases ( Imentioning

confidence: 99%

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Amino Acid Selection in Protein Biosynthesis

Peterson¹

1967

Biological Reviews

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Section: ( E ) Sulphur Amino Acidsmentioning

confidence: 98%

Section: (I) Species Occurrencesmentioning

confidence: 99%

Section: ( E ) Sulphur Amino Acidsmentioning

confidence: 99%

Section: Additional Properties Of Aminoacyl-s-rna Synthetases ( Imentioning

confidence: 99%

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Amino Acid Selection in Protein Biosynthesis

Peterson¹

1967

Biological Reviews

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“…Ethionine, the S-ethyl analog of methionine, is incorporated into proteins in Escherichia coli, B. subtilis, and other organisms (1,5,6,13,22,40). The eucaryotic S-adenosylmethionine (SAM) synthetases (ATP:L-methionine S-adenosyltransferase, EC 2.5.1.6) use ethionine as a substrate in the synthesis of S-adenosylethionine (SAE) (6,12,16,30,33). But ethionine is not a substrate for the SAM synthetases of E. coli or Salmonella typhimurium (7,17,23).…”

mentioning

confidence: 99%

An ethA mutation in Bacillus subtilis 168 permits induction of sporulation by ethionine and increases DNA modification of bacteriophage phi 105

Allen¹,

Orrego²,

Wabiko³

et al. 1986

J Bacteriol

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In contrast to Escherichia coli and SalmoneUa typhimurium, BaciUus subtilis could convert ethionine to S-adenosylethionine (SAE), as can Saccharomyces cerevisiae. This conversion was essential for growth inhibition by ethionine because metE mutants which were deficient in S-adenosylmethionine synthetase activity, were resistant to 10 mM ethionine and converted only a smiall amount of ethionine to SAE. Another mutation (ethAl) produced partial resistance to ethionine (2 mM) and enabled continual sporulation in glucose medium containing 4 mM DL-ethionine. This sporulation induction probably resulted from the effect of SAE, since it was abolished by the addition of a metE) mutation. The induction of sporulation was not simply controlled by the ratio of SAE to S-adenosylmethionine, but apparently depended on another effect of the ethAl mutation, which could be demonstrated by comparing the restriction of clear plaque mutants of bacteriophage +105 grown in an ethAl strain with the restriction of those grown in the standard strain. The phages grown in the ethAl strain showed increased 'protection against BsuR restriction. We propose that SAE induces sporulation through the inhibition of a key methylation reaction.Vegetative cells of Bacillus subtilis differentiate into heatresistant endospores when the composition of the growth medium becomes insufficient to sustain rapid growth. Numerous conditions which cause massive sporulation have been described (10,11,25,29); investigations of nucleotide changes reveal that a sudden drop in the intracellular concentration of GTP and GDP occurs at the onset of sporulation induced by each of these conditions. Furthermore, the use of both specific inhibitors and mutations affecting only the guanine pathway has shown that this decrease is sufficient to induce mnassive sporulation (11,24). Ochi et al. (28) found that the addition of methionine analogs (either ethionine or selenomethionine) to cultures of B. subtilis also induces sporulation. In these experiments, they used a relA strain to avoid induction of sporulation by the stringent response. This paper investigates the effect of ethionine, the more effective of the two analogs, in more detail. Ethionine, the S-ethyl analog of methionine, is incorporated into proteins in Escherichia coli, B. subtilis, and other organisms (1,5,6,13,22,40). The eucaryotic S-adenosylmethionine (SAM) synthetases (ATP:L-methionine S-adenosyltransferase, EC 2.5.1.6) use ethionine as a substrate in the synthesis of S-adenosylethionine (SAE) (6,12,16,30,33). But ethionine is not a substrate for the SAM synthetases of E. coli or Salmonella typhimurium (7,17,23). In vitro, SAE inhibits SAM-dependent DNA modification (4). We show here that B. subtilis converted ethionine to SAE and that it was SAE which was responsible for the inhibition of growth and the induction of sporulatiori. (27). Therefore, we reasoned that the mutant cells (those having an ethAl mutation) might have altered activity of an essential modification enzyme which would ensure methylati...

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Biochemical Basis for Ethionine Effects on Tissues

Stekol

1963

Advances in Enzymology - And Related Areas of Molecular Biology

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Activation of l-methionine and l-ethionine by pH 5 fraction of rat liver

Cited by 24 publications

References 10 publications

Amino Acid Selection in Protein Biosynthesis

Amino Acid Selection in Protein Biosynthesis

An ethA mutation in Bacillus subtilis 168 permits induction of sporulation by ethionine and increases DNA modification of bacteriophage phi 105

Biochemical Basis for Ethionine Effects on Tissues

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