Tags

Type your tag names separated by a space and hit enter

Regulation of acetate metabolism in Corynebacterium glutamicum: transcriptional control of the isocitrate lyase and malate synthase genes.
Arch Microbiol. 1997 Oct; 168(4):262-9.AM

Abstract

In the amino-acid-producing microorganism Corynebacterium glutamicum, the specific activities of the acetate-activating enzymes acetate kinase and phosphotransacetylase and those of the glyoxylate cycle enzymes isocitrate lyase and malate synthase were found to be high when the cells were grown on acetate (0.8, 2.9, 2.1, and 1.8 U/mg protein, respectively). When the cells were grown on glucose or on other carbon sources such as lactate, succinate, or glutamate, the specific activities were two- to fourfold (acetate kinase and phosphotransacetylase) and 45- to 100-fold (isocitrate lyase and malate synthase) lower, indicating that the synthesis of the four enzymes is regulated by acetate in the growth medium. A comparative Northern (RNA) analysis of the C. glutamicum isocitrate lyase and malate synthase genes (aceA and aceB) and transcriptional cat fusion experiments revealed that aceA and aceB are transcribed as 1.6- and 2.7-kb monocistronic messages, respectively, and that the regulation of isocitrate lyase and malate synthase synthesis is exerted at the level of transcription from the respective promoters. Surprisingly, C. glutamicum mutants defective in either acetate kinase or phosphotransacetylase showed low specific activities of the other three enzymes (phosphotransacetylase, isocitrate lyase, and malate synthase or acetate kinase, isocitrate lyase, and malate synthase, respectively) irrespective of the presence or absence of acetate in the medium. This result and a correlation of a high intracellular acetyl coenzyme A concentration with high specific activities of isocitrate lyase, malate synthase, acetate kinase, and phosphotransacetylase suggest that acetyl coenzyme A or a derivative thereof may be a physiological trigger for the genetic regulation of enzymes involved in acetate metabolism of C. glutamicum.

Authors+Show Affiliations

Wendisch VF
Institut für Biotechnologie 1, Forschungszentrum Jülich, D-52425 Jülich, Germany.
Spies M
No affiliation info available
Reinscheid DJ
No affiliation info available
Schnicke S
No affiliation info available
Sahm H
No affiliation info available
Eikmanns BJ
No affiliation info available

MeSH

Acetate KinaseAcetatesAcetyl Coenzyme AArtificial Gene FusionBlotting, NorthernCloning, MolecularCorynebacteriumGene Expression Regulation, BacterialGene Expression Regulation, EnzymologicGlucoseGlutamic AcidIsocitrate LyaseLactatesMalate SynthasePhosphate AcetyltransferasePlasmidsRestriction MappingSuccinic AcidTranscription, GeneticTransformation, Genetic

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

9297462

Citation

Wendisch, V F., et al. "Regulation of Acetate Metabolism in Corynebacterium Glutamicum: Transcriptional Control of the Isocitrate Lyase and Malate Synthase Genes." Archives of Microbiology, vol. 168, no. 4, 1997, pp. 262-9.
Wendisch VF, Spies M, Reinscheid DJ, et al. Regulation of acetate metabolism in Corynebacterium glutamicum: transcriptional control of the isocitrate lyase and malate synthase genes. Arch Microbiol. 1997;168(4):262-9.
Wendisch, V. F., Spies, M., Reinscheid, D. J., Schnicke, S., Sahm, H., & Eikmanns, B. J. (1997). Regulation of acetate metabolism in Corynebacterium glutamicum: transcriptional control of the isocitrate lyase and malate synthase genes. Archives of Microbiology, 168(4), 262-9.
Wendisch VF, et al. Regulation of Acetate Metabolism in Corynebacterium Glutamicum: Transcriptional Control of the Isocitrate Lyase and Malate Synthase Genes. Arch Microbiol. 1997;168(4):262-9. PubMed PMID: 9297462.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Regulation of acetate metabolism in Corynebacterium glutamicum: transcriptional control of the isocitrate lyase and malate synthase genes. AU - Wendisch,V F, AU - Spies,M, AU - Reinscheid,D J, AU - Schnicke,S, AU - Sahm,H, AU - Eikmanns,B J, PY - 1997/9/23/pubmed PY - 1997/9/23/medline PY - 1997/9/23/entrez SP - 262 EP - 9 JF - Archives of microbiology JO - Arch Microbiol VL - 168 IS - 4 N2 - In the amino-acid-producing microorganism Corynebacterium glutamicum, the specific activities of the acetate-activating enzymes acetate kinase and phosphotransacetylase and those of the glyoxylate cycle enzymes isocitrate lyase and malate synthase were found to be high when the cells were grown on acetate (0.8, 2.9, 2.1, and 1.8 U/mg protein, respectively). When the cells were grown on glucose or on other carbon sources such as lactate, succinate, or glutamate, the specific activities were two- to fourfold (acetate kinase and phosphotransacetylase) and 45- to 100-fold (isocitrate lyase and malate synthase) lower, indicating that the synthesis of the four enzymes is regulated by acetate in the growth medium. A comparative Northern (RNA) analysis of the C. glutamicum isocitrate lyase and malate synthase genes (aceA and aceB) and transcriptional cat fusion experiments revealed that aceA and aceB are transcribed as 1.6- and 2.7-kb monocistronic messages, respectively, and that the regulation of isocitrate lyase and malate synthase synthesis is exerted at the level of transcription from the respective promoters. Surprisingly, C. glutamicum mutants defective in either acetate kinase or phosphotransacetylase showed low specific activities of the other three enzymes (phosphotransacetylase, isocitrate lyase, and malate synthase or acetate kinase, isocitrate lyase, and malate synthase, respectively) irrespective of the presence or absence of acetate in the medium. This result and a correlation of a high intracellular acetyl coenzyme A concentration with high specific activities of isocitrate lyase, malate synthase, acetate kinase, and phosphotransacetylase suggest that acetyl coenzyme A or a derivative thereof may be a physiological trigger for the genetic regulation of enzymes involved in acetate metabolism of C. glutamicum. SN - 0302-8933 UR - https://www.unboundmedicine.com/medline/citation/9297462/Regulation_of_acetate_metabolism_in_Corynebacterium_glutamicum:_transcriptional_control_of_the_isocitrate_lyase_and_malate_synthase_genes_ L2 - https://dx.doi.org/10.1007/s002030050497 DB - PRIME DP - Unbound Medicine ER -