Derepression of the glyoxylate cycle in mutants of Neurospora crassa accelerated for growth on acetate

Article Abstract:

The Aag-1 (accelerated acetate growth) mutants of Neurospora crassa grow faster than the wild strain if the carbon source is acetate but slower if the carbon source is sucrose. In the presence of sucrose acetyl-CoA synthetase enzymes involved in the glyoxylate cycle are stimulated but other enzymes are unaffected. The concentration of these enzymes in the cells increases due to uncontrolled transcription which allows the cells to use acetate better and grow faster.

author: Connerton, I.F., Chaure, P.T.
Analysis, Growth, Acetates, Neurospora

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The erg-3 (sterol delta(super 14,15-reductase)) gene of Neurospora crassa: generation of null mutants by repeat-induced point mutation and complementation by proteins chimeric for human lamin B receptor sequences

Article Abstract:

A study was conducted to determine whether the lamin b receptor transmembrane domain can function as a delta(super 14,15)-reductase. Recombinant genes that encode proteins which were chimeras of N. crassa erg-3 were constructed. Results indicated that the erg-3 mutant could be complemented by transformation with recombinant genes that encode proteins chimeric for amino acid sequences from the transmembrane domain of the receptor.

author: Kasbekar, Durgadas P., Aparna, K., Prakash, A., Sengupta, Saswati
Flavonoids, Flavones, Oxidation-reduction reaction, Oxidation-reduction reactions

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Isolation of mutants deficient in acetyl-CoA synthetase and a possible regulator of acetate induction in Aspergillus niger

Article Abstract:

Research was conducted to examine acetate-non-utilizing mutants in Aspergillus niger. Mutants that exhibited normal morphology were classified into two complementation groups. One class featured reduced levels of isocitrate lyase and acetyl-CoA synthetase compared with the wild-type strain. The other class did not have acetyl-CoA synthetase but had high levels of isocitrate lyase.

author: Sealy-Lewis, Heather M., Fairhurst, Valerie
Aspergillus, Microbial enzymes

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subjects list: Research
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