Production of
            <scp>l</scp>
            -Arginine by Arginine Hydroxamate-Resistant Mutants of
            <i>Bacillus subtilis</i>

Kisumi, Masahiko; Sugiura, Masaki; Chibata, Ichiro

doi:10.1128/am.22.6.987-991.1971

Cited by 14 publications

(3 citation statements)

References 24 publications

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“…Glu-HXM, a toxic analog of glutamic acid, and arginine hydroxamate, a toxic analog of arginine, are inhibitors of arginine metabolism, while ammonium sulfate and urea are nitrogen sources that are component parts of the pathway ( Fig. 5e ) ( Kisumi et al . 1971 ; Vila et al .…”

Section: Resultsmentioning

confidence: 99%

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Profiling the compendium of changes in Saccharomyces cerevisiae due to mutations that alter availability of the main methyl donor S-Adenosylmethionine

Remines,

Schoonover,

Knox

et al. 2024

G3: Genes, Genomes, Genetics

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The SAM1 and SAM2 genes encode for S-AdenosylMethionine (AdoMet) synthetase enzymes, with AdoMet serving as the main cellular methyl donor. We have previously shown that independent deletion of these genes alters chromosome stability and AdoMet concentrations in opposite ways in Saccharomyces cerevisiae. To characterize other changes occurring in these mutants, we grew wildtype, sam1Δ/sam1Δ, and sam2Δ/sam2Δ strains in 15 different Phenotypic Microarray plates with different components and measured growth variations. RNA-Sequencing was also carried out on these strains and differential gene expression determined for each mutant. We explored how the phenotypic growth differences are linked to the altered gene expression, and hypothesize mechanisms by which loss of the SAM genes and subsequent AdoMet level changes, impact pathways and processes. We present six stories, discussing changes in sensitivity or resistance to azoles, cisplatin, oxidative stress, arginine biosynthesis perturbations, DNA synthesis inhibitors, and tamoxifen, to demonstrate the power of this novel methodology to broadly profile changes due to gene mutations. The large number of conditions that result in altered growth, as well as the large number of differentially expressed genes with wide-ranging functionality, speaks to the broad array of impacts that altering methyl donor abundance can impart. Our findings demonstrate that some cellular changes are directly related to AdoMet-dependent methyltransferases and AdoMet availability, some are directly linked to the methyl cycle and its role in production of several important cellular components, and others reveal impacts of SAM gene mutations on previously unconnected pathways.

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Section: Resultsmentioning

confidence: 99%

“…Arginine hydroxamate inhibits arginine biosynthesis, but it has been found that increased concentrations of ornithine and citrulline, produced within the urea cycle, are able to reverse the inhibitory effect ( Fig. 5e ) ( Kisumi et al . 1971 ).…”

Section: Resultsmentioning

confidence: 99%

Profiling the compendium of changes in Saccharomyces cerevisiae due to mutations that alter availability of the main methyl donor S-Adenosylmethionine

Remines,

Schoonover,

Knox

et al. 2024

G3: Genes, Genomes, Genetics

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“…Amino acid analogue arginine hyroxamate inhibited the growth by different bacteria and also reversed in the presence of arginine amino acid [14]. In order to isolate arginine analogue resistant mutant initially, the minimum inhibitory concentration of arginine hydroxamate was determined by tube dilution method.…”

Section: Mutagenesismentioning

confidence: 99%

Production of L-Arginine from arginine analogue resistant mutants of Corynebacterium glutamicum

Musini¹,

Mangamoori²,

Saida³

2018

IJSRBS

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L-arginine is an essential amino acid, widely used in pharmaceutical, feed and food industry. It is the precursor molecule in citrulline and nitric oxide synthesis, which in turn plays significant role in a wide variety of patho -physiological functions in the cardiovascular, central and peripheral nervous systems. In the present study, mutagenesis experiments were carried out for isolation of analogue resistant mutants against Corynebacterium glutamicum. Initially, MIC (Minimum inhibitory concentration) was identified for arginine analogues by tube dilution method. MIC values found to be Arginine hydroximate -680 µg/ml. Further, mutagenesis of C. glutamicum was carried out with NTG (300µg/ml) and amino acid analogue resistant mutants were isolated in minimal media. Fermentation was carried out by resistant colonies and estimated the Arginine levels. Production level was found to be 5.2 mg /ml where as in control cells it was 1.4 mg /ml. This study highlighted the C. glutamicum mutant of L-arginine amino acid production.

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Recent advances in industrial fermentation in Japan

Yamada

1977

Biotech & Bioengineering

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Production of l -Arginine by Arginine Hydroxamate-Resistant Mutants of Bacillus subtilis

Cited by 14 publications

References 24 publications

Profiling the compendium of changes in Saccharomyces cerevisiae due to mutations that alter availability of the main methyl donor S-Adenosylmethionine

Profiling the compendium of changes in Saccharomyces cerevisiae due to mutations that alter availability of the main methyl donor S-Adenosylmethionine

Production of L-Arginine from arginine analogue resistant mutants of Corynebacterium glutamicum

Recent advances in industrial fermentation in Japan

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