The flavoproteome of the yeast Saccharomyces cerevisiae
| Autor: | Venugopal, Gudipati, Karin, Koch, Wolf-Dieter, Lienhart, Peter, Macheroux |
|---|---|
| Rok vydání: | 2013 |
| Předmět: |
Saccharomyces cerevisiae Proteins
Flavoproteins Proteome Q ubiquionone ETC electron transport chain DRAP 2 5-diamino-6-(ribosylamino)-4-(3H)-pyrimidinone 5′-phosphate Biological Transport Review DHBP 3 4-dihydroxy-2-butanone-4-phosphate Iron metabolism Gly3p glycerol 3-phosphate tRNA-modifications ER endoplasmic reticulum Redox balance DHAP dihydroxy acetone phosphate ORF open reading frame Membrane transporters Mia(40) mitochondrial intermembrane space import and assay/oxidoreductase 40 Flavins Humans Mitochondrion Oxidation-Reduction gluSA γ-glutamic acid semialdehyde |
| Zdroj: | Biochimica et Biophysica Acta |
| ISSN: | 0006-3002 |
| Popis: | Genome analysis of the yeast Saccharomyces cerevisiae identified 68 genes encoding flavin-dependent proteins (1.1% of protein encoding genes) to which 47 distinct biochemical functions were assigned. The majority of flavoproteins operate in mitochondria where they participate in redox processes revolving around the transfer of electrons to the electron transport chain. In addition, we found that flavoenzymes play a central role in various aspects of iron metabolism, such as iron uptake, the biogenesis of iron–sulfur clusters and insertion of the heme cofactor into apocytochromes. Another important group of flavoenzymes is directly (Dus1-4p and Mto1p) or indirectly (Tyw1p) involved in reactions leading to tRNA-modifications. Despite the wealth of genetic information available for S. cerevisiae, we were surprised that many flavoproteins are poorly characterized biochemically. For example, the role of the yeast flavodoxins Pst2p, Rfs1p and Ycp4p with regard to their electron donor and acceptor is presently unknown. Similarly, the function of the heterodimeric Aim45p/Cir1p, which is homologous to the electron-transferring flavoproteins of higher eukaryotes, in electron transfer processes occurring in the mitochondrial matrix remains to be elucidated. This lack of information extends to the five membrane proteins involved in riboflavin or FAD transport as well as FMN and FAD homeostasis within the yeast cell. Nevertheless, several yeast flavoproteins, were identified as convenient model systems both in terms of their mechanism of action as well as structurally to improve our understanding of diseases caused by dysfunctional human flavoprotein orthologs. Highlights • Overview of flavin-dependent proteins in S. cerevisiae. • The role of yeast flavoproteins in iron metabolism. • Biosynthesis and transport of flavins. • Yeast as a model organism for investigating human diseases linked to flavoproteins. |
| Databáze: | OpenAIRE |
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