Cold‐induced increase of glycerol kinase in <i>Neurospora crassa</i>

North, Michael

doi:10.1016/0014-5793(73)80578-2

Cited by 25 publications

(13 citation statements)

References 12 publications

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“…Currently, three glycerol metabolic pathways have been reported [24], one phosphorylative pathway [25], [26] and two oxidative pathways that are based on NAD(P) + -dependent glycerol dehydrogenases [27]. In this report, we have identified and characterized the first eukaryotic TSR and demonstrated its role in glycerol catabolism and production of glycolipids from glycerol (Figure 5, 6, S3, S4, Table 2).…”

Section: Discussionmentioning

confidence: 80%

Tartronate Semialdehyde Reductase Defines a Novel Rate-Limiting Step in Assimilation and Bioconversion of Glycerol in Ustilago maydis

et al. 2011

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BackgroundGlycerol is a by-product of biodiesel production. Currently, it has limited applications with low bioconversion efficiency to most metabolites reported. This is partly attributed to the poor knowledge on the glycerol metabolic pathway in bacteria and fungi.Methodology/Principal FindingsWe have established a fast screening method for identification of genes that improve glycerol utilization in Ustilago maydis. This was done by comparing the growth rates of T-DNA tagged mutant colonies on solid medium using glycerol as the sole carbon source. We present a detailed characterization of one of the mutants, GUM1, which contains a T-DNA element inserted into the promoter region of UM02592 locus (MIPS Ustilago maydis database, MUMDB), leading to enhanced and constitutive expression of its mRNA. We have demonstrated that um02592 encodes a functional tartronate semialdehyde reductase (Tsr1), which showed dual specificity to cofactors NAD+ and NADP+ and strong substrate specificity and enantioselectivity for D-glycerate. Improved glycerol assimilation in GUM1 was associated with elevated expression of tsr1 mRNA and this could be phenocopied by over-expression of the gene. Glycolipid accumulation was reduced by 45.2% in the knockout mutant whereas introduction of an extra copy of tsr1 driven by the glyceraldehyde phosphate dehydrogenase promoter increased it by 40.4%.Conclusions/SignificanceOur results demonstrate that tartronate semialdehyde reductase (TSR) plays an important role in glycerol assimilation in U. maydis and defines a novel target in genetic engineering for improved conversion of glycerol to higher value products. Our results add significant depth to the understanding of the glycerol metabolic pathway in fungi. We have demonstrated, for the first time, a biological role of a eukaryotic TSR.

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Section: Discussionmentioning

confidence: 80%

Tartronate Semialdehyde Reductase Defines a Novel Rate-Limiting Step in Assimilation and Bioconversion of Glycerol in Ustilago maydis

et al. 2011

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“…Ullrich and Heber (1961) found that five soluble enzymes which were not sedimented by centrifuging, were neither coagulated nor inactivated by freezing. In fact freezing is used as a routine method for isolating them (Rhodes and Stewart, 1974), to preserve them (Judel, 1975), or even to activate them (North, 1973;Sheppard and Tsien, 1974). McCown et a/.…”

Section: B Relation To Enzyme Inactivationmentioning

confidence: 99%

Molecular Basis of Freezing Injury and Tolerance

Levitt

1980

Chilling, Freezing, and High Temperature Stresses

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“…B. Courtright, Bacteriol. Proc., p. 153, 1971), but also by lowering the growth temperature of cultures growing on sucrose as sole carbon source (22). In this report, evidence is presented for a rapid inactivation in vivo of glycerol kinase.…”

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confidence: 93%

Cold-Induced Increase of Glycerol Kinase Activity in Neurospora crassa : Rapid Inactivation of the Enzyme In Vivo

North

1974

J Bacteriol

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The glycerol kinase activity induced by incubation of Neurospora crassa at low temperatures was rapidly lost when cultures were returned to 26 C. After a short lag, the activity disappeared irreversibly with a half-life of approximately 15 min. The loss of activity was not due, to a change in the level of an inhibitor or activator. Glycerol reduced the activity loss but did not completely prevent it, which was an effect that was dependent on protein synthesis. The cold-induced activity was also always lost on addition of cycloheximide at all temperatures tested (O to 26 C), which indicated continuous inactivation, although cycloheximide did not affect the actual rate of activity loss at 26 C. The basal glycerol kinase activity was not sensitive to cycloheximide. The mechanism responsible for inactivation was destroyed by sonic oscillation. The process is not thought to play a role in the cold-induced increase in activity. Glycerol kinase activity induced at 26 C by glycerol was also lost on addition of cycloheximide and after addition of sucrose.

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Cold‐induced increase of glycerol kinase in Neurospora crassa

Cited by 25 publications

References 12 publications

Tartronate Semialdehyde Reductase Defines a Novel Rate-Limiting Step in Assimilation and Bioconversion of Glycerol in Ustilago maydis

Tartronate Semialdehyde Reductase Defines a Novel Rate-Limiting Step in Assimilation and Bioconversion of Glycerol in Ustilago maydis

Molecular Basis of Freezing Injury and Tolerance

Cold-Induced Increase of Glycerol Kinase Activity in Neurospora crassa : Rapid Inactivation of the Enzyme In Vivo

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