Inhibition and repression of homocitrate synthase by lysine in Penicillium chrysogenum

Luengo, José M.; Revilla, Gloría; López, Mario; Villanueva, Julio R.; Martı́n, Juan F.

doi:10.1128/jb.144.3.869-876.1980

Cited by 71 publications

(19 citation statements)

References 19 publications

(16 reference statements)

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“…We found that emetic toxin production was sharply decreased in the media supplemented with a high concentration of leucine, isoleucine or glutamic acid. This finding is similar to previous observations that the production of a botulinum neurotoxin was suppressed by high levels of certain amino acids (8,10), and that the biosynthesis of antibiotic penicillin was negatively regulated by several amino acids (3,7).…”

Section: Discussionsupporting

confidence: 92%

Growth Conditions of and Emetic Toxin Production by Bacillus cereus in a Defined Medium with Amino Acids

Agata¹,

Ohta

Mori³

et al. 1999

Microbiology and Immunology

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The growth and emetic toxin (cereulide) production of Bacillus cereus strains in defined culture media were studied. We found that a fully synthetic medium (CADM) allowed the production of emetic toxin and the addition of glucose enhanced it. By subtracting each amino acid from CADM, we found that only three amino acids, valine, leucine and threonine, were essential for growth and toxin production by B. cereus. The addition of high levels (50 mm) of leucine, isoleucine and glutamic acid decreased the toxin production. Other amino acids had no effect at this concentration.

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Section: Discussionsupporting

confidence: 92%

Growth Conditions of and Emetic Toxin Production by Bacillus cereus in a Defined Medium with Amino Acids

Agata¹,

Ohta

Mori³

et al. 1999

Microbiology and Immunology

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“…Consistent with this assumption was the notion that in P. chrysogenum, one target for lysine regulation is homocitrate synthase, which catalyzes the initial reaction of lysine biosynthesis. Lysine was found to cause both feedback inhibition of homocitrate synthase activity and repression of its synthesis (14,26). In agreement with these findings, it was shown that the AA pool available for penicillin production was reduced in lysine-grown mycelia (23,38).…”

supporting

confidence: 60%

Regulation of the Aspergillus nidulans Penicillin Biosynthesis Gene acvA ( pcbAB ) by Amino Acids: Implication for Involvement of Transcription Factor PACC

Bergh¹,

Brakhage²

1998

Appl Environ Microbiol

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The β-lactam antibiotic penicillin is produced as an end product by some filamentous fungi only. It is synthesized from the amino acid precursors l-α-aminoadipic acid, l-cysteine, and l-valine. Previous data suggested that certain amino acids play a role in the regulation of its biosynthesis. Therefore, in this study the effects of externally added amino acids on bothAspergillus (Emericella) nidulanspenicillin production and expression of the bidirectionally oriented biosynthesis genes acvA (pcbAB) andipnA (pcbC) were comprehensively investigated. Different effects caused by amino acids on the expression of penicillin biosynthesis genes and penicillin production were observed. Amino acids with a major negative effect on the expression of acvA-uidAand ipnA-lacZ gene fusions, i.e., histidine, valine, lysine, and methionine, led to a decreased ambient pH during cultivation of the fungus. An analysis of deletion clones lacking binding sites for the pH-dependent transcriptional factor PACC in the intergenic regions between acvA-uidA andipnA-lacZ gene fusions and in a pacC5 mutant (PacC5-5) suggested that the negative effects of histidine and valine on acvA-uidA expression were due to reduced activation by PACC under acidic conditions. These data also implied that PACC regulates the expression of acvA, predominantly through PACC binding site ipnA3. The repressing effect caused by lysine and methionine on acvA expression, however, was even enhanced in one of the deletion clones and the pacC5 mutant strain, suggesting that regulators other than PACC are also involved.

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“…When the binding ['4C]NeuAc to proteins was analysed, reaction mixtures were precipitated with 10 % (w/v) trichloroacetic acid as described by Luengo et al (1980). The trichloroacetic acid solution was cooled to 0°C for 10 min and centrifuged at 5000 g for 5 min.…”

Section: Sialyltransferase Activitymentioning

confidence: 99%

A protein-sialyl polymer complex involved in colominic acid biosynthesis. Effect of tunicamycin

Rodrı́guez-Aparicio

Reglero

Ortiz

et al. 1988

Biochemical Journal

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A protein-NeuAc complex involved in colominic acid biosynthesis has been identified in membrane preparations of Escherichia coli K-235. This compound had an Mr (estimated by SDS/polyacrylamide-gel electrophoresis and autoradiography) of about 100,000 and played the role of an 'initiator' or 'primer' (endogenous acceptor) in the synthesis of the whole polymer. Incubations of E. coli membranes with CMP-[14C]NeuAc (CMP-N-[14C]acetylneuraminic acid) pointed to the existence of a protein fraction (primer acceptor) that linked residues of sialic acid (N-acetylneuraminic acid, NeuAc) up to a maximal size, later releasing them as low-Mr sialyl polymers (LMrS, Mr less than 10,000). In the presence of colominic acid (final acceptor) the radioactivity linked to the protein quickly decreased, appearing stoichiometrically bound to the whole polysaccharide. When membrane preparations were previously digested with Streptomyces proteinase or de-activated by heating (80 degrees C, 10 min), no incorporation of labelled NeuAc into trichloroacetic acid-insoluble material was detected. These results suggested that colominic acid molecules are synthesized while they are bound to a proteinaceous acceptor that is subsequently excised in the presence of colominic acid, generating the native protein. The antibiotic tunicamycin inhibited the biosynthesis of colominic acid, affecting the synthesis of this protein-(NeuAc)n intermediate. All these results are described here for the first time.

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Inhibition and repression of homocitrate synthase by lysine in Penicillium chrysogenum

Cited by 71 publications

References 19 publications

Growth Conditions of and Emetic Toxin Production by Bacillus cereus in a Defined Medium with Amino Acids

Growth Conditions of and Emetic Toxin Production by Bacillus cereus in a Defined Medium with Amino Acids

Regulation of the Aspergillus nidulans Penicillin Biosynthesis Gene acvA ( pcbAB ) by Amino Acids: Implication for Involvement of Transcription Factor PACC

A protein-sialyl polymer complex involved in colominic acid biosynthesis. Effect of tunicamycin

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