De novo synthesis and desaturation of fatty acids at the mitochondrial acyl‐carrier protein, a subunit of NADH:ubiquinone oxidoreductase in <i>Neurospora crassa</i>

Zensen, Ralf; Husmann, H.; Schneider, Ralf; Peine, Thorsten; Weiss, Hanns

doi:10.1016/0014-5793(92)81324-f

Cited by 53 publications

(33 citation statements)

References 12 publications

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“…Both of these conditions showed that the longest predominant fatty acid synthesized by mitochondria is C16. There has been some speculation on the use of mitochondrially synthesized fatty acids in lysophospholipid repair (57) or synthesis of cardiolipin (58). Indeed, we can detect phospholipid-related species whose synthesis may be dependant on mitochondrial FAS (threonine-labeled phospholipids are reduced following induction of ACP RNAi (Fig.…”

Section: Discussionmentioning

confidence: 90%

Mitochondrial Fatty Acid Synthesis in Trypanosoma brucei

Stephens¹,

Lee²,

Paul³

et al. 2007

Journal of Biological Chemistry

111

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Whereas other organisms utilize type I or type II synthases to make fatty acids, trypanosomatid parasites such as Trypanosoma brucei are unique in their use of a microsomal elongase pathway (ELO) for de novo fatty acid synthesis (FAS). Because of the unusual lipid metabolism of the trypanosome, it was important to study a second FAS pathway predicted by the genome to be a type II synthase. We localized this pathway to the mitochondrion, and RNA interference (RNAi) or genomic deletion of acyl carrier protein (ACP) and ␤-ketoacyl-ACP synthase indicated that this pathway is likely essential for bloodstream and procyclic life cycle stages of the parasite. In vitro assays show that the largest major fatty acid product of the pathway is C16, whereas the ELO pathway, utilizing ELOs 1, 2, and 3, synthesizes up to C18. To demonstrate mitochondrial FAS in vivo, we radiolabeled fatty acids in cultured procyclic parasites with

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Section: Discussionmentioning

confidence: 90%

Mitochondrial Fatty Acid Synthesis in Trypanosoma brucei

Stephens¹,

Lee²,

Paul³

et al. 2007

Journal of Biological Chemistry

111

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“…The occurrence of a FAS system in mitochondria was first implied by the discovery of a mitochondrially located ACP in Neurospora crassa (Zensen et al, 1992). Since then, this FAS system has been characterized in yeast and humans (Hiltunen et al, 2010), confirming its multicomponent, type II character.…”

Section: Discussionmentioning

confidence: 97%

Discovery and Characterization of the 3-Hydroxyacyl-ACP Dehydratase Component of the Plant Mitochondrial Fatty Acid Synthase System

et al. 2017

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We report the characterization of the Arabidopsis (Arabidopsis thaliana) 3-hydroxyacyl-acyl carrier protein dehydratase (mtHD) component of the mitochondrial fatty acid synthase (mtFAS) system, encoded by AT5G60335. The mitochondrial localization and catalytic capability of mtHD were demonstrated with a green fluorescent protein transgenesis experiment and by in vivo complementation and in vitro enzymatic assays. RNA interference (RNAi) knockdown lines with reduced mtHD expression exhibit traits typically associated with mtFAS mutants, namely a miniaturized morphological appearance, reduced lipoylation of lipoylated proteins, and altered metabolomes consistent with the reduced catalytic activity of lipoylated enzymes. These alterations are reversed when mthd-rnai mutant plants are grown in a 1% CO 2 atmosphere, indicating the link between mtFAS and photorespiratory deficiency due to the reduced lipoylation of glycine decarboxylase. In vivo biochemical feeding experiments illustrate that sucrose and glycolate are the metabolic modulators that mediate the alterations in morphology and lipid accumulation. In addition, both mthd-rnai and mtkas mutants exhibit reduced accumulation of 3-hydroxytetradecanoic acid (i.e. a hallmark of lipid A-like molecules) and abnormal chloroplastic starch granules; these changes are not reversible by the 1% CO 2 atmosphere, demonstrating two novel mtFAS functions that are independent of photorespiration. Finally, RNA sequencing analysis revealed that mthd-rnai and mtkas mutants are nearly equivalent to each other in altering the transcriptome, and these analyses further identified genes whose expression is affected by a functional mtFAS system but independent of photorespiratory deficiency. These data demonstrate the nonredundant nature of the mtFAS system, which contributes unique lipid components needed to support plant cell structure and metabolism.

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“…Mitochondrial fatty acid synthesis and the involvement of a type II ACP in this process were originally observed by Brody and coworkers in Neurospora crassa (15,91). 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).…”

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

confidence: 93%

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

Schweizer

Hofmann

2004

Microbiol Mol Biol Rev

325

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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De novo synthesis and desaturation of fatty acids at the mitochondrial acyl‐carrier protein, a subunit of NADH:ubiquinone oxidoreductase in Neurospora crassa

Cited by 53 publications

References 12 publications

Mitochondrial Fatty Acid Synthesis in Trypanosoma brucei

Mitochondrial Fatty Acid Synthesis in Trypanosoma brucei

Discovery and Characterization of the 3-Hydroxyacyl-ACP Dehydratase Component of the Plant Mitochondrial Fatty Acid Synthase System

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

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