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The Formation of hybrid complexes between isoenzymes of glyceraldehyde-3-phosphate dehydrogenase regulates its aggregation state, the glycolytic activity and sphingolipid status in Saccharomyces cerevisiae

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The Formation of hybrid complexes between isoenzymes of glyceraldehyde-3-phosphate dehydrogenase regulates its aggregation state, the glycolytic activity and sphingolipid status in Saccharomyces cerevisiae

dc.contributor.author	Rández Gil, Francisca
dc.contributor.author	Sánchez‐Adriá, Isabel E.
dc.contributor.author	Estruch Ros, Francisco
dc.contributor.author	Prieto Alamán, José Antonio
dc.date.accessioned	2021-03-24T15:09:03Z
dc.date.available	2021-03-24T15:09:03Z
dc.date.issued	2020
dc.identifier.citation	Rández-Gil, Francisca Sánchez&#8208Adriá, Isabel E. Estruch Ros, Francisco Prieto Alamán, José Antonio 2020 The Formation of hybrid complexes between isoenzymes of glyceraldehyde-3-phosphate dehydrogenase regulates its aggregation state, the glycolytic activity and sphingolipid status in Saccharomyces cerevisiae Microbial Biotechnology 13 2 562 571
dc.identifier.uri	https://hdl.handle.net/10550/78350
dc.description.abstract	The glycolytic enzyme glyceraldehyde-3-phosphate dehydrogenase (GAPDH) has been traditionally considered a housekeeping protein involved in energy generation. However, evidence indicates that GAPDHs from different origins are tightly regulated and that this regulation may be on the basis of glycolysis-related and glycolysis-unrelated functions. In Saccharomyces cerevisiae, Tdh3 is the main GAPDH, although two other isoenzymes encoded by TDH1 and TDH2 have been identified. Like other GAPDHs, Tdh3 exists predominantly as a tetramer, although dimeric and monomeric forms have also been isolated. Mechanisms of Tdh3 regulation may thus imply changes in its oligomeric state or be based in its ability to interact with Tdh1 and/or Tdh2 to form hybrid complexes. However, no direct evidence of the existence of these interactions has been provided and the exact function of Tdh1,2 is unknown. Here, we show that Tdh1,2 immunopurified with a GFP-tagged version of Tdh3 and that lack of this interaction stimulates the Tdh3's aggregation. Furthermore, we found that the combined knockout of TDH1 and TDH2 promotes the loss of cell's viability and increases the growing rate, glucose consumption and CO2 production, suggesting a higher glycolytic flux in the mutant cells. Consistent with this, the tdh3 strain, which displays impaired in vitro GAPDH activity, exhibited the opposite phenotypes. Quite remarkably, tdh1 tdh2 mutant cells show increased sensitivity to aureobasidin A, an inhibitor of the inositolphosphoryl ceramide synthase, while cells lacking Tdh3 showed improved tolerance. The results are in agreement with a link between glycolysis and sphingolipid (SLs) metabolism. Engineering Tdh activity could be thus exploited to alter the SLs status with consequences in different aspects of yeast biotechnology.
dc.language.iso	eng
dc.relation.ispartof	Microbial Biotechnology, 2020, vol. 13, num. 2, p. 562-571
dc.subject	Microbiologia
dc.subject	Enzims
dc.title	The Formation of hybrid complexes between isoenzymes of glyceraldehyde-3-phosphate dehydrogenase regulates its aggregation state, the glycolytic activity and sphingolipid status in Saccharomyces cerevisiae
dc.type	journal article	es_ES
dc.date.updated	2021-03-24T15:09:03Z
dc.identifier.doi	10.1111/1751-7915.13513
dc.identifier.idgrec	138838
dc.rights.accessRights	open access	es_ES