The ORF YNL274c (GOR1) codes for glyoxylate reductase in Saccharomyces cerevisiae

Rintala, Eija; Pitkänen, Juha-Pekka; Vehkomäki, Maija-Leena; Penttilä, Merja; Ruohonen, Laura

doi:10.1002/yea.1434

Cited by 18 publications

(13 citation statements)

References 30 publications

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“…Our Basic Local Alignment Search Tool (BLAST) search against the protein database of yeast Saccharomyces cerevisiae revealed that YNL274C (a NADPH-dependent glyoxylate reductase) is most similar to dCtBP, although it lacks the PXDLS-and RRT-binding motifs (Rintala et al 2007). So far, worms appear to be the simplest animal that contains CtBP.…”

Section: Resultsmentioning

confidence: 98%

Structurally related Arabidopsis ANGUSTIFOLIA is functionally distinct from the transcriptional corepressor CtBP

et al. 2007

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ANGUSTIFOLIA (AN) controls leaf morphology in the plant Arabidopsis thaliana. Previous studies on sequence similarity demonstrated that the closest proteins to AN are members of animal C-terminal-binding proteins (CtBPs) found in nematodes, arthropods, and vertebrates. Drosophila CtBP (dCtBP) functions as a transcriptional corepressor for deoxyribonucleic acid (DNA)-binding repressors containing the short amino acid motif, PXDLS, to regulate tissue specification and segmentation during early embryogenesis. It has previously been shown that AN was thought to repress transcription similar to the function of CtBPs; however, AN lacks some of the structural features that are conserved in animal CtBPs. In this paper, we examined whether AN is functionally related to dCtBP. Firstly, we re-examined sequence similarity among AN and various CtBPs from several representative species in the plant and animal kingdoms. Secondly, yeast two-hybrid assays demonstrated that AN failed to interact with an authentic CtBP-interacting factor, adenovirus E1A oncoprotein bearing the PXDLS motif. Thirdly, AN tethered to DNA was unable to repress the expression of reporter genes in transgenic Drosophila embryos. Fourthly, overexpression assays suggested that dCtBP and AN function differently in Drosophila tissues. Finally, AN failed to rescue the zygotic lethality caused by dCtBP loss-of-function. These data, taken together, suggest that AN is functionally distinct from dCtBP. Likely, ancestral CtBPs acquired corepressor function (capability of both repression and binding to repressors containing the PXDLS motif) after the animal-plant divergence but before the protostome-deuterostome split. We therefore propose to categorize AN as a subfamily member within the CtBP/BARS/RIBEYE/AN superfamily.

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Section: Resultsmentioning

confidence: 98%

Structurally related Arabidopsis ANGUSTIFOLIA is functionally distinct from the transcriptional corepressor CtBP

et al. 2007

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“…The activity of the endogenous S. cerevisiae glyoxylate reductase GOR1 [13] and the A. thaliana GLYR1 [14] he GLYR1 gene was codon optimised for expression in yeast. Both genes were overexpressed in S. cerevisiae from the same multicopy plasmid and the activity with glyoxylic acid and NADPH was measured from crude extracts.…”

Section: Resultsmentioning

confidence: 99%

“…In S. cerevisiae , two glyoxylate reductase isoforms have been purified [23,24] but only one gene, GOR1 , encoding glyoxylate reductase activity has been identified [13]. Deletion of the glyoxylate reductase, GOR1 , led to increased biomass formation after diauxic shift, which was thought to be caused by increased NADPH availability [13].…”

Section: Discussionmentioning

confidence: 99%

“…Deletion of the glyoxylate reductase, GOR1 , led to increased biomass formation after diauxic shift, which was thought to be caused by increased NADPH availability [13]. The biological function of the enzyme is not clear but it may have a role in glyoxylate detoxification as has been described for plants [15].…”

Section: Discussionmentioning

confidence: 99%

“…The work demonstrates that glycolic acid can be produced from the glyoxylate cycle through the reduction of glyoxylate to glycolic acid using a glyoxylate reductase enzyme. S. cerevisiae has a gene coding for a NADPH specific glyoxylate reductase, GOR1 , which is not expressed under normal growth conditions and has a low affinity for glyoxylate [13]. A higher affinity for glyoxylate has been reported for the glyoxylate reductase, GLYR1, from Arabidopsis thaliana [14] that is also NADPH requiring.…”

Section: Introductionmentioning

confidence: 99%

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Glycolic acid production in the engineered yeasts Saccharomyces cerevisiae and Kluyveromyces lactis

et al. 2013

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BackgroundGlycolic acid is a C2 hydroxy acid that is a widely used chemical compound. It can be polymerised to produce biodegradable polymers with excellent gas barrier properties. Currently, glycolic acid is produced in a chemical process using fossil resources and toxic chemicals. Biotechnological production of glycolic acid using renewable resources is a desirable alternative.ResultsThe yeasts Saccharomyces cerevisiae and Kluyveromyces lactis are suitable organisms for glycolic acid production since they are acid tolerant and can grow in the presence of up to 50 g l-1 glycolic acid. We engineered S. cerevisiae and K. lactis for glycolic acid production using the reactions of the glyoxylate cycle to produce glyoxylic acid and then reducing it to glycolic acid. The expression of a high affinity glyoxylate reductase alone already led to glycolic acid production. The production was further improved by deleting genes encoding malate synthase and the cytosolic form of isocitrate dehydrogenase. The engineered S. cerevisiae strain produced up to about 1 g l-1 of glycolic acid in a medium containing d-xylose and ethanol. Similar modifications in K. lactis resulted in a much higher glycolic acid titer. In a bioreactor cultivation with d-xylose and ethanol up to 15 g l-1 of glycolic acid was obtained.ConclusionsThis is the first demonstration of engineering yeast to produce glycolic acid. Prior to this work glycolic acid production through the glyoxylate cycle has only been reported in bacteria. The benefit of a yeast host is the possibility for glycolic acid production also at low pH, which was demonstrated in flask cultivations. Production of glycolic acid was first shown in S. cerevisiae. To test whether a Crabtree negative yeast would be better suited for glycolic acid production we engineered K. lactis in the same way and demonstrated it to be a better host for glycolic acid production.

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Current awareness on yeast

2007

Yeast

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In order to keep subscribers up‐to‐date with the latest developments in their field, this current awareness service is provided by John Wiley & Sons and contains newly‐published material on yeasts. Each bibliography is divided into 10 sections. 1 Reviews; 2 General; 3 Biochemistry; 4 Biotechnology; 5 Cell Biology; 6 Gene Expression; 7 Genetics; 8 Physiology; 9 Medical Mycology; 10 Recombinant DNA Technology. Within each section, articles are listed in alphabetical order with respect to author. If, in the preceding period, no publications are located relevant to any one of these headings, that section will be omitted. (4 weeks journals ‐ search completed 4th. Apr. 2007)

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The ORF YNL274c (GOR1) codes for glyoxylate reductase in Saccharomyces cerevisiae

Cited by 18 publications

References 30 publications

Structurally related Arabidopsis ANGUSTIFOLIA is functionally distinct from the transcriptional corepressor CtBP

Structurally related Arabidopsis ANGUSTIFOLIA is functionally distinct from the transcriptional corepressor CtBP

Glycolic acid production in the engineered yeasts Saccharomyces cerevisiae and Kluyveromyces lactis

Current awareness on yeast

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