Soluble fumarate reductase isoenzymes from Saccharomyces cerevisiae are required for anaerobic growth

Arikawa, Yukihiko

doi:10.1016/s0378-1097(98)00260-2

Cited by 15 publications

(22 citation statements)

References 16 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…We further found that both OSM1 and FRD1, encoding fumarate reductase, were upregulated under anaerobic conditions. It was reported that a single deletion of either OSM1 or FRD1 does not affect the anaerobic cell growth (40), whereas a double deletion is lethal under anaerobic conditions but has no growth effect under aerobic conditions (41), and it was suggested that fumarate reductase is essential under anaerobic conditions because it catalyzes the only reaction that could oxidize free FADH 2 under these conditions (40). Here, we propose that the FAD that is reduced to FADH 2 by accepting electrons from protein folding in the ER is then oxidized back to FAD by the fumarate reductase.…”

Section: Figmentioning

confidence: 99%

Anaerobic α-Amylase Production and Secretion with Fumarate as the Final Electron Acceptor in Saccharomyces cerevisiae

Liu

Österlund

Hou

et al. 2013

Appl Environ Microbiol

View full text Add to dashboard Cite

bIn this study, we focus on production of heterologous ␣-amylase in the yeast Saccharomyces cerevisiae under anaerobic conditions. We compare the metabolic fluxes and transcriptional regulation under aerobic and anaerobic conditions, with the objective of identifying the final electron acceptor for protein folding under anaerobic conditions. We find that yeast produces more amylase under anaerobic conditions than under aerobic conditions, and we propose a model for electron transfer under anaerobic conditions. According to our model, during protein folding the electrons from the endoplasmic reticulum are transferred to fumarate as the final electron acceptor. This model is supported by findings that the addition of fumarate under anaerobic (but not aerobic) conditions improves cell growth, specifically in the ␣-amylase-producing strain, in which it is not used as a carbon source. Our results provide a model for the molecular mechanism of anaerobic protein secretion using fumarate as the final electron acceptor, which may allow for further engineering of yeast for improved protein secretion under anaerobic growth conditions.

show abstract

Section: Figmentioning

confidence: 99%

Anaerobic α-Amylase Production and Secretion with Fumarate as the Final Electron Acceptor in Saccharomyces cerevisiae

Liu

Österlund

Hou

et al. 2013

Appl Environ Microbiol

View full text Add to dashboard Cite

show abstract

“…Recently, we constructed disruptants of the FRDS and OSM1 genes [9,10]. The OSM1 disruptant (DOSM) grew more slowly than DBY747 under anaerobic conditions, and the disruptant of both the FRDS and OSM1 genes (DFRDOSM) failed to grow at all.…”

Section: Introductionmentioning

confidence: 99%

Physiological role of soluble fumarate reductase in redox balancing during anaerobiosis in Saccharomyces cerevisiae

Enomoto¹

2002

FEMS Microbiology Letters

View full text Add to dashboard Cite

In Saccharomyces cerevisiae, there are two isoenzymes of fumarate reductase (FRDS1 and FRDS2), encoded by the FRDS and OSM1 genes, respectively. Simultaneous disruption of these two genes results in a growth defect of the yeast under anaerobic conditions, while disruption of the OSM1 gene causes slow growth. However, the metabolic role of these isoenzymes has been unclear until now. In the present study, we found that the anaerobic growth of the strain disrupted for both the FRDS and OSM1 genes was fully restored by adding the oxidized form of methylene blue or phenazine methosulfate, which non-enzymatically oxidize cellular NADH to NAD þ . When methylene blue was added at growth-limiting concentrations, growth was completely arrested after exhaustion of oxidized methylene blue. In the double-disrupted strain, the accumulation of succinate in the supernatant was markedly decreased during anaerobic growth in the presence of methylene blue. These results suggest that fumarate reductase isoenzymes are required for the reoxidation of intracellular NADH under anaerobic conditions, but not aerobic conditions.

show abstract

Section: Introductionmentioning

confidence: 99%

Physiological role of soluble fumarate reductase in redox balancing during anaerobiosis inSaccharomyces cerevisiae

Enomoto

Arikawa

Muratsubaki

2002

FEMS Microbiology Letters

View full text Add to dashboard Cite

In Saccharomyces cerevisiae, there are two isoenzymes of fumarate reductase (FRDS1 and FRDS2), encoded by the FRDS and OSM1 genes, respectively. Simultaneous disruption of these two genes results in a growth defect of the yeast under anaerobic conditions, while disruption of the OSM1 gene causes slow growth. However, the metabolic role of these isoenzymes has been unclear until now. In the present study, we found that the anaerobic growth of the strain disrupted for both the FRDS and OSM1 genes was fully restored by adding the oxidized form of methylene blue or phenazine methosulfate, which non-enzymatically oxidize cellular NADH to NAD(+). When methylene blue was added at growth-limiting concentrations, growth was completely arrested after exhaustion of oxidized methylene blue. In the double-disrupted strain, the accumulation of succinate in the supernatant was markedly decreased during anaerobic growth in the presence of methylene blue. These results suggest that fumarate reductase isoenzymes are required for the reoxidation of intracellular NADH under anaerobic conditions, but not aerobic conditions.

show abstract

Soluble fumarate reductase isoenzymes from Saccharomyces cerevisiae are required for anaerobic growth

Cited by 15 publications

References 16 publications

Anaerobic α-Amylase Production and Secretion with Fumarate as the Final Electron Acceptor in Saccharomyces cerevisiae

Anaerobic α-Amylase Production and Secretion with Fumarate as the Final Electron Acceptor in Saccharomyces cerevisiae

Physiological role of soluble fumarate reductase in redox balancing during anaerobiosis in Saccharomyces cerevisiae

Physiological role of soluble fumarate reductase in redox balancing during anaerobiosis inSaccharomyces cerevisiae

Contact Info

Product

Resources

About