Metabolism of Sulfur Compounds
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Like S. Kluyveromyces thermotolerans, K. BAT2 of L. Eremothecium gossypii, D. Pichia stipitis only have the cytoplasmic enzyme Bat2p, the latter species carrying a duplication of this gene. The evolution of these genes in fungi is complex and needs to be extensively explored in relation to the functions they are associated with.
Phylogenetic analysis of aromatic aminotransferases differentiated three groups of proteins, one of them being associated to the S.
This group comprises potential aromatic amino acid aminotransferases. This gene is well conserved, with one copy in each genome and a duplication in K. The strong conservation of this gene leads us to infer that this gene might play an important role under specific conditions. All these aromatic transaminases seem to be cytoplasmic except the Aro9 enzyme in Y.
In the ARO8 group, a duplication event apparently occurred after the divergence of the group constituted of E.
At least one copy of ARO8 is in fact present in all the tested species. The presence of the gene ARO9 seems to follow different routes. In fact, this gene has been lost in two species, E. Phylogram of the aminotransferases of the Aro8p and Aro9p families and of the related Yercp-like family in hemiascomycetous yeasts. The Saccharomyces cerevisiae proteins are boxed. We identified three combinations of the five enzymes described above Bat1, Bat2, Aro8, Aro9, Yerc in the hemiascomycetes. The first, which has all five of these enzymes, is found in S.
Metabolism of Sulfur Compounds
The second, observed in Z. The third lacks Bat1 and Aro9 and is found in E. Thus, two enzymes are always present in all these yeasts — Aro8 and Yerc — stressing the importance of the aminotransferase Aro8 and of the protein of unknown function, Yerc. We observed that each of the three technological yeasts, K. This could be indicative of different potentialities for the biosynthesis of VSC in these three yeasts. Methional is an important molecule for cheese flavor.
This sulfur compound is a product of methionine degradation from KMBA, the first intermediary of methionine catabolism. This enzyme belongs to a large family of decarboxylases including the pyruvate decarboxylases. This enzyme has been described as an orthologue of PDC1 but seems to be closer to PDC6 according to this study data not shown. This regulator not only plays a central role in the regulation of the sulfur amino acid biosynthetic pathway, but in the cell cycle as well.
The latter is an ubiquitination complex composed of Skp1, Cdc53, Cdc34, Rbx1 and Met30 as specific components. It can be observed that there is no orthologue of RBX1 in the N. CBF1 is conserved in all species studied, but the blastp analysis reveals a sequence alignment only in the C-terminal region.
This table represents the sequence similarity percentages for each regulatory protein studied, in comparison with Saccharomyces cerevisiae.
Oxidative metabolism of inorganic sulfur compounds by bacteria | SpringerLink
The analysis was carried out using the gap software from gcg Accelrys Inc. Met4 orthologues display large differences among the species studied. The family of MET4 -related genes can be separated into two subfamilies: a family of large polypeptides related to S. This second family is related to fungal regulators such as Cys3 and MetR from N. We can raise the question whether or not these orthologues carry all the interaction domains such as Met4 from S. One argument for the conservation of these interactions is that the partners of Met4 are globally conserved except for Met28, which appeared to be absent in the clade of the short-length Met4 subfamily.
However, the shorter Met4 sequences display a canonical BZIP motif with a basic region, allowing direct interaction with DNA, and a leucine zipper required for dimerization. Therefore, Met28, which is not conserved in the studied species, appears to have an ancillary function. The activation motif of S. Conversely, the motif upstream from the ubiquitinated lysine K in S. However, it is difficult to identify the sites of interaction with these regulators when distant Met4 orthologues are analyzed.
For instance, in Y. In conclusion, it seems that the coregulation network depicted in S. It is clear that these hypotheses should be validated by mutagenesis experiments. An overview of the sulfur amino acid pathways in hemiascomycetous yeasts was generated. It was important to investigate whether the wealth of data accumulated in the model yeast S. By and large, the pathways appeared to be conserved even beyond the yeast world, in the whole phylum of fungi.
This is probably foreseeable as this pathway plays a central role in the general metabolism and homeostasis of the cell. Moreover, we propose that the regulation network in charge of the sulfur amino acid biosynthesis and its central component Met4 are conserved from S. All the other partners appeared to be conserved along the evolutionary tree, especially Met31 and Met30, which play a central role in the specificity of the regulation. It is tempting to investigate a conservation of these binding sites along the evolutionary tree. This binding site is shared with several transcription factors: Pho4, which belongs to the phosphate regulon Gonze, , Rtg3, a TOR-controlled transcription activator, Tye7, a transcription factor involved in the activation of glycolytic enzymes Zhu, Moreover, Cormier have recently studied the PDC6 promoter which belongs to a subclass of promoters responding to a starvation in sulfur amino acids induced by cadmium stress Fauchon, This effect was shown to be fully dependent on the presence of the transcription factors of the Met regulon: Met4, Met32 and Cbf1.
These data from S. But we were unable to find the same combination of sites in a similar set of genes from K. Cbf1-like sites were easily found but they are very frequent in these genomes, as in S. We have therefore investigated the presence of such a binding site in the promoters of the MET regulon in Yarrowia.
It is therefore difficult to give a firm answer on the specificity of the interaction between Met4 homologues and their specific promoters without experimental studies. The majority of the studied species possess two pathways leading to cysteine production, the transsulfuration pathway and the OAS pathway, except S.
Summary of the components of the sulfur amino acids pathway highlighting the differences in cysteine synthesis according to the yeast clades. The study of the gene families involved in this metabolism were conducted to identify well-conserved gene families without described function, although they are highly conserved and they diverge at the same speed as the essential genes of the pathway. This is also the case in the catabolic pathway for the YERc gene family related to the aromatic amino acid aminotransferase family without identified function in S.
Their conservation during evolution suggests an important role for them in the metabolism of the sulfur compounds. Concerning the catabolism of sulfur amino acids that leads to the production of VSC, the technological yeasts K. The results of this work remain to be confirmed by genetic and molecular studies. All authors read and approved the manuscript. Appendix S1.
Oxidative metabolism of inorganic sulfur compounds by bacteria
List of genes involved in sulfur metabolism in each species studied. Appendix S2. Table of proteins studied. Please note: Wiley-Blackwell is not responsible for the content or functionality of any supporting materials supplied by the authors. Any queries other than missing material should be directed to the corresponding author for the article. Oxford University Press is a department of the University of Oxford.
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Supporting Information. Oxford Academic. Google Scholar. Serge Casaregola. Jean-Marie Beckerich. Editor: Monique Bolotin-Fukuhara. Cite Citation. Permissions Icon Permissions. Abstract The evolution of the metabolism of sulfur compounds among yeast species was investigated. Open in new tab Download slide. Open in new tab. Search ADS. Fitting a mixture model by expectation maximization to discover motifs in biopolymers.