Sulphate activation and its control in <i>Escherichia coli</i> and <i>Bacillus subtilis</i>

Ca, Pasternak

doi:10.1042/bj0850044

Cited by 50 publications

(31 citation statements)

References 15 publications

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“…Incorporation of radiosulphate into various micro-organisms is prevented by cysteine (Roberts et al 1957;Pasternak, 1962). Jn the case of Escherichia coli, however, cystine was used instead of cysteine, since the former compound fails to inhibit the growth of E. coli.…”

Section: Efect Of Cysteine On [35s]-sulphate Incorporationmentioning

confidence: 99%

Mechanism of the Growth Inhibitory Effect of Cysteine on Escherichia coli

Kari

Nagy

Kovács

et al. 1971

Journal of General Microbiology

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S U M M A R YCysteine appeared to have two classes of growth inhibitory effect onEscherichia coli: (I) above 0.2 m i t inhibited growth on minimal medium by a mechanism which may involve interference with leucine, isoleucine, threonine and valine biosynthesis ; ( 2 ) above 2 mM, in media with these amino acids, it had an effect which may involve interaction with membrane bound respiratory enzymes.Cysteamine showed only effect ( 2 ) . I N T R O D U C T I O NRoberts, Abelson, Cowie, Bolton & Britten (1957) reported that exogenous cysteine inhibits the growth of Escherichia coli, but the mechanism of this action is still unclarified. Nagy, Hernadi, Kovhcs, Valyi-Nagy (1968a) and Nagy, Kovacs, Kari & Hernidi (1970) found that, in E. coli 1 5~-, the net synthesis of RNA and protein, but not that of DNA, was quickly inhibited by cysteine. An antagonism could be detected between cysteine and leucine (leu), isoleucine (ileu), threonine (threo) and valine (Val) and it was suggested that the biosynthesis of these amino acids (AAs) is inhibited by cysteine (Kovhcs, Kari, Nagy & Hernidi, 1968). However, not all the effects of cysteine could be explained in this way (Nagy, Kari & Hernadi, 1969 Hernadi, 1971). Each of these effects may be responsible for its cytotoxic action, but it is difficult to demonstrate which of these many reactions is involved in growth inhibition. Enzyme experiments in vitro and the various metabolic actions of cysteine need to be assessed in the light of detailed growth studies. M E T H O D SBacterial strains, Escherichia coli strain B (prototroph, from T. Alper of Hammersmith Hospital, London) ; Hfr CAVALLI met-rel-(a relaxed strain, auxotrophic for methionine) ; CP 99 his-arg-ser-Bl-reE+ (a stringent strain, auxotrophic for histidine, arginine, serine and B~) ; and CPIOO his-arg-ser-B,-rel-(a relaxed mutant of ~~9 9 ) .The latter three strains were obtained from L. Alfoldi (Medical University of Szeged, Hungary).Growth. Organisms were cultivated on mineral salts medium C (Roberts et al. 1957)

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Section: Efect Of Cysteine On [35s]-sulphate Incorporationmentioning

confidence: 99%

Mechanism of the Growth Inhibitory Effect of Cysteine on Escherichia coli

Kari

Nagy

Kovács

et al. 1971

Journal of General Microbiology

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“…The complete process of assimilatory sulfate reduction supplies prototrophic organisms with reduced sulfur as required for the biosynthesis of all sulfur-containing metabolites. The assimilatory reduction of sulfate and formation of cysteine have been extensively studied in Escherichia coli and Salmonella typhimurium (13,15,24,25). At least 22 genes required for the transport and reduction of sulfate and its incorporation into cysteine have been identified in these bacteria (15).…”

mentioning

confidence: 99%

“…It has been reported that high levels of cysteine biosynthetic enzymes are found in E. coli and S. typhimurium cells grown on minimal medium containing a poor sulfate source, such as glutathione, and that low levels are found in cells grown on good sulfur sources such as sulfide and cysteine (13,24,25).…”

mentioning

confidence: 99%

L-cysteine biosynthesis in Bacillus subtilis: identification, sequencing, and functional characterization of the gene coding for phosphoadenylylsulfate sulfotransferase

Mansilla

Mendoza

1997

J Bacteriol

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Random Tn917 mutagenesis of Bacillus subtilis followed by selection of lipoic acid auxotrophs led to the isolation of the cysH gene. The gene was sequenced and found to encode a phosphoadenylylsulfate sulfotransferase with a molecular mass of 27 kDa. Expression of lacZ fused to the cysH promoter was repressed by cysteine and sulfide and induced by sulfur limitation, indicating that cysH is controlled at the level of transcription.

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“…The effect of methionine on 36S incorporation into cysteine may not be due to a direct inhibition. Pasternak (1961) and Ellis & Pasternak (1962) observed repression of sulphate activation by growth with cysteine in E . coli and a weaker repression effect with methionine.…”

Section: Discussionmentioning

confidence: 97%

Studies of Methionine Synthesis in Coprinus lagopus

Clark

Rowbury

1964

Journal of General Microbiology

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SUMMARYWhen methionine was present in the growth medium of wild-type Coprinus lagopus the incorporation of isotope from 35S-sulphate into both cysteine and methionine was greatly decreased. Under these conditions much of the cysteine formed must have arisen from methionine and it is concluded that the diminution of cysteine synthesis from sulphate is caused by the cysteine formed from the methionine and not directly by methionine itself.Wild-type Coprinus accumulated large amounts of cystathionine when grown with methionine and this appeared to have arisen from the added methionine as isotope from 35S-sulphate was not incorporated into the accumulated compound. The cysteine formed from methionine may have been formed from this accumulated cystathionine.

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Sulphate activation and its control in Escherichia coli and Bacillus subtilis

Cited by 50 publications

References 15 publications

Mechanism of the Growth Inhibitory Effect of Cysteine on Escherichia coli

Mechanism of the Growth Inhibitory Effect of Cysteine on Escherichia coli

L-cysteine biosynthesis in Bacillus subtilis: identification, sequencing, and functional characterization of the gene coding for phosphoadenylylsulfate sulfotransferase

Studies of Methionine Synthesis in Coprinus lagopus

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