<i>Candida tropicalis</i> Etr1p and<i>Saccharomyces cerevisiae</i> Ybr026p (Mrf1′p), 2-Enoyl Thioester Reductases Essential for Mitochondrial Respiratory Competence

Torkko, Juha M.; Koivuranta, Kari; Miinalainen, Ilkka; Yagi, Ahmed; Schmitz, W.; Kastaniotis, Alexander J.; Airenne, Tomi T.; Gurvitz, Aner; Hiltunen, Kalervo

doi:10.1128/mcb.21.18.6243-6253.2001

Cited by 76 publications

(101 citation statements)

References 53 publications

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“…This strongly suggests that the corresponding translation products do encode mitochondrially localised products. This point has been recently confirmed for COQ4 (Belogrudov et al, 2001) and MRF1′ (Torkko et al, 2001).…”

Section: In Vivo Localization Of Mrnas Of High Mlr Valuesupporting

confidence: 50%

Genome‐wide analysis of mRNAs targeted to yeast mitochondria

et al. 2002

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It is agreed that nuclear-encoded mitochondrial proteins are post-translationally targeted to mitochondria, even if, in some cases, a co-translational phase can assist the import of precursor proteins. We used yeast DNA microarrays to analyse the mRNA populations associated with free and mitochondrion-bound polysomes. As expected, many mRNAs, known to encode mitochondrial proteins, are localized to free cytoplasmic polysomes, but many are localized to mitochondrion-bound polysomes. Furthermore, the 3′-UTR of six randomly chosen mitochondrion-bound mRNAs contains sufficient information to target, in vivo, non-translatable RNA to the vicinity of mitochondria. Interestingly, genes producing mRNAs that are targeted to mitochondria are mainly of ancient bacterial origin, whereas those producing mRNAs that are translated in the cytoplasm are mainly of eukaryotic origin. These observations, which support the recent hypotheses concerning the dual origin of the mitochondrial proteome, provide new insights into the biogenesis of mitochondria.

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Section: In Vivo Localization Of Mrnas Of High Mlr Valuesupporting

confidence: 50%

Genome‐wide analysis of mRNAs targeted to yeast mitochondria

et al. 2002

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“…Subsequently, it was demonstrated by several groups (116,117,187) (48). The screening of the S. cerevisiae genome by different groups finally led to the identification of essentially all the components of a bacterial type II FAS encoded by nuclear genes but obviously located in the mitochondrial compartment (16,122,164). Discovering that in Neurospora and mammals, one of the central components of prokaryotic FAS, i.e., ACP, was part of the respiratory chain was rather puzzling at first.…”

Section: Multiple Fatty Acid Synthases In Yeast and Other Fungi Mitocmentioning

confidence: 99%

Microbial Type I Fatty Acid Synthases (FAS): Major Players in a Network of Cellular FAS Systems

Schweizer

Hofmann

2004

Microbiol Mol Biol Rev

321

286

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The present review focuses on microbial type I fatty acid synthases (FASs), demonstrating their structural and functional diversity. Depending on their origin and biochemical function, multifunctional type I FAS proteins form dimers or hexamers with characteristic organization of their catalytic domains. A single polypeptide may contain one or more sets of the eight FAS component functions. Alternatively, these functions may split up into two different and mutually complementing subunits. Targeted inactivation of the individual yeast FAS acylation sites allowed us to define their roles during the overall catalytic process. In particular, their pronounced negative cooperativity is presumed to coordinate the FAS initiation and chain elongation reactions. Expression of the unlinked genes, FAS1 and FAS2, is in part constitutive and in part subject to repression by the phospholipid precursors inositol and choline. The interplay of the involved regulatory proteins, Rap1, Reb1, Abf1, Ino2/Ino4, Opi1, Sin3 and TFIIB, has been elucidated in considerable detail. Balanced levels of subunits α and β are ensured by an autoregulatory effect of FAS1 on FAS2 expression and by posttranslational degradation of excess FAS subunits. The functional specificity of type I FAS multienzymes usually requires the presence of multiple FAS systems within the same cell. De novo synthesis of long-chain fatty acids, mitochondrial fatty acid synthesis, acylation of certain secondary metabolites and coenzymes, fatty acid elongation, and the vast diversity of mycobacterial lipids each result from specific FAS activities. The microcompartmentalization of FAS activities in type I multienzymes may thus allow for both the controlled and concerted action of multiple FAS systems within the same cell

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“…Plants synthesize fatty acids within the plastids, and use a discrete and highly conserved group of dissociated enzymes named fatty acid synthase system type 2 (FASII) [6]. This system, similarily to the eukaryotic mitochondrial FAS [7][8][9][10], differs from the mammalian cytosolic fatty acid synthase system type 1 (FASI) where all reactions are carried out by a single multifunctional polypeptide [11]. Fatty acids synthesized within plastid are exported to endoplasmic reticulum (ER) for elongation, resulting in the formation of VLCFAs that are essential cellular precursors of waxes, seed storage lipids and sphingolipids [5].…”

Section: Introductionmentioning

confidence: 99%

Cloning and functional characterization of two cDNAs encoding NADPH-dependent 3-ketoacyl-CoA reductased from developing cotton fibers

et al. 2005

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Genes encoding enzymes involved in biosynthesis of very long chain fatty acids were significantly up-regulated during early cotton fiber development. Two cDNAs, GhKCR1 and GhKCR2 encoding putative cotton 3-ketoacyl-CoA reductases that catalyze the second step in fatty acid elongation, were isolated from developing cotton fibers. GhKCR1 and 2 contain open reading frames of 963 bp and 924 bp encoding proteins of 320 and 307 amino acid residues, respectively. Quantatitive RT-PCR analysis showed that both these genes were highly preferentially expressed during the cotton fiber elongation period with much lower levels recovered from roots, stems and leaves. GhKCR1 and 2 showed 30%-32% identity to Saccharomyces cerevisiae Ybr159p at the deduced amino acid level. These cotton cDNAs were cloned and expressed in yeast haploid ybr159w∆ mutant that was deficient in 3-ketoacyl-CoA reductase activity. Wild-type growth rate was restored in ybr159w∆ cells that expressed either GhKCR1 or 2. Further analysis showed that GhKCR1 and 2 were co-sedimented within the membranous pellet fraction after high-speed centrifugation, similar to the yeast endoplasmic reticulum marker ScKar2p. Both GhKCR(s) showed NADPH-dependent 3-ketoacyl-CoA reductase activity in an in vitro assay system using palmitoyl-CoA and malonyl-CoA as substrates. Our results suggest that GhKCR1 and 2 are functional orthologues of ScYbr159p.

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Candida tropicalis Etr1p andSaccharomyces cerevisiae Ybr026p (Mrf1′p), 2-Enoyl Thioester Reductases Essential for Mitochondrial Respiratory Competence

Cited by 76 publications

References 53 publications

Genome‐wide analysis of mRNAs targeted to yeast mitochondria

Genome‐wide analysis of mRNAs targeted to yeast mitochondria

Microbial Type I Fatty Acid Synthases (FAS): Major Players in a Network of Cellular FAS Systems

Cloning and functional characterization of two cDNAs encoding NADPH-dependent 3-ketoacyl-CoA reductased from developing cotton fibers

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