Understanding the function of bacterial and eukaryotic thiolases II by integrating evolutionary and functional approaches

Fox, Ana Romina; Soto, Gabriela; Mozzicafreddo, Matteo; García, Araceli Nora; Cuccioloni, Massimiliano; Angeletti, Mauro; Salerno, J. C.; Ayub, Nicolás Daniel

doi:10.1016/j.gene.2013.09.096

Cited by 24 publications

(19 citation statements)

References 44 publications

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“…Moreover, these differential pathways could be installed in series, and the EC 2.3.1.9 and EC 2.6.1.21 participating in these metabolic pathways were highly expressed in the Hce group. EC 2.3.1.9 (Acetoacetyl-CoA thiolase) catalyzes the cleavage of acetoacetyl-CoA into acetyl-CoA and its reverse reaction ( Fox et al, 2014 ), and EC 2.6.1.21 ( D -Amino acid aminotransferase) catalyzes the inter-conversion between various D -amino acids and alpha-keto acids ( Fuchikami et al, 1998 ). They are responsible for fatty acid degradation and potentially produce medium chain fatty acids for energy supplementation, helping growth of the host.…”

Section: Discussionmentioning

confidence: 99%

Metagenomic Analysis of Cecal Microbiome Identified Microbiota and Functional Capacities Associated with Feed Efficiency in Landrace Finishing Pigs

et al. 2017

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Feed efficiency (FE) appears to vary even within closely related pigs, and may be partly affected by the diversity in the composition and function of gut microbes. To investigate the components and functional differences of gut microbiota of low and high FE pigs, high throughput sequencing and de novo metagenomics were performed on pig cecal contents. Pigs were selected in pairs with low and high feed conversion ratio. The microorganisms of individuals with different FE were clustered according to diversity. The genus Prevotella was the most enriched in both groups, and the abundance of species Prevotella sp. CAG:604 was significantly increased in low efficiency individuals compared to that in animals showing high efficiency. In contrast, other differential species, including lactic acid bacteria, were all enriched in the group with good feeding characteristics. Functional analysis based on the Kyoto Encyclopedia of Genes and Genomes databases demonstrated that differential genes for the metabolism of carbohydrates were most abundant in both groups, but pathways of pyruvate-related metabolism were more intense in pigs with higher FE. All these data indicated that the microbial environment was closely related to the growth traits of pigs, and regulating microbial composition could aid developing strategies to improve FE for pigs.

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Section: Discussionmentioning

confidence: 99%

Metagenomic Analysis of Cecal Microbiome Identified Microbiota and Functional Capacities Associated with Feed Efficiency in Landrace Finishing Pigs

et al. 2017

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“…PHB is a biopolymer synthesized by a wide range of microbes as a way to store energy, which, consequently, displays important roles in bacterial survival under starvation conditions (Lopez et al, 1995). Consistent with this intracellular function, PHB is generally produced in the cytoplasm and involves a three-step synthesis, commonly known as the ABC pathway (Fox et al, 2014) (Fig. 2a-b).…”

Section: Resultsmentioning

confidence: 95%

“…For example, peroxisomal and cytosolic thiolases II are extremely similar enzymes (>85 % of amino acid identity) but display catabolic (e.g. fatty acid β-oxidation) and anabolic (mevalonate biosynthesis) functions, respectively (Fox et al, 2014;Soto et al, 2011). Although it is well known that functional divergence after gene duplication is sometimes related to a switch in the subcellular localization of an enzyme, the molecular mechanisms involved in this switch are unknown.…”

Section: Introductionmentioning

confidence: 99%

Understanding the intracellular-to-extracellular localization switch of polyhydroxybutyrate polymerase in pseudomonas backgrounds as a microevolutionary process

Stritzler

Berini

Jozefkowicz

et al. 2018

Journal of Theoretical Biology

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After gene duplication, paralogous genes evolve independently, and consequently, the new proteins encoded by these duplicated genes are exposed to changes in their subcellular location. Although there are increasing evidence that phylogenetically related proteins play different functions in different subcellular compartments, the number of evolutionary steps required for the emergence of a novel protein with a novel subcellular localization remains unclear. Regarding this intriguing topic, here we examine in depth our previous reports describing both intracellular and extracellular polyhydroxybutyrate polymerases (PhaC) in the Pseudomonadales group. The recapitulation of the intracellular-to-extracellular localization switch of PhaC in these strains shows a gradual evolution from a simple cytosolic PhaC form to a complex extracellular PhaC form specifically secreted via the type 1 secretion system. This gradual evolution includes several adaptive and pre-adaptive changes at the genomic, genetic and enzymatic levels, which are intimately related to the lifestyle of organisms during the evolution of protein localization. We conclude that the protein localization switch can be an extremely complex process in nature.

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“…Condensation between two acetyl-CoA molecules to form acetoacetyl-CoA has been recognized as the first step in the mevalonate pathway in eukaryotes [3]. This reaction is catalyzed through a non-decarboxylative Claisen-type condensation by an enzyme that belongs to the thiolase protein family known as acetyl-CoA C-acetyltransferase (ACAT) [4, 5].…”

Section: Introductionmentioning

confidence: 99%

Functional characterization of thiolase-encoding genes from Xanthophyllomyces dendrorhous and their effects on carotenoid synthesis

et al. 2016

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BackgroundThe basidiomycetous yeast Xanthophyllomyces dendrorhous has been described as a potential biofactory for terpenoid-derived compounds due to its ability to synthesize astaxanthin. Functional knowledge of the genes involved in terpenoid synthesis would create opportunities to enhance carotenoid production. A thiolase enzyme catalyzes the first step in terpenoid synthesis.ResultsTwo potential thiolase-encoding genes were found in the yeast genome; bioinformatically, one was identified as an acetyl-CoA C-acetyltransferase (ERG10), and the other was identified as a 3-ketoacyl Co-A thiolase (POT1). Heterologous complementation assays in Saccharomyces cerevisiae showed that the ERG10 gene from X. dendrorhous could complement the lack of the endogenous ERG10 gene in S. cerevisiae, thereby allowing cellular growth and sterol synthesis. X. dendrorhous heterozygous mutants for each gene were created, and a homozygous POT1 mutant was also obtained. This mutant exhibited changes in pigment composition and higher ERG10 transcript levels than the wild type strain.ConclusionsThe results support the notion that the ERG10 gene in X. dendrorhous is a functional acetyl-CoA C-acetyltransferase essential for the synthesis of mevalonate in yeast. The POT1 gene would encode a functional 3-ketoacyl Co-A thiolase that is non-essential for cell growth, but its mutation indirectly affects pigment production.Electronic supplementary materialThe online version of this article (doi:10.1186/s12866-016-0893-2) contains supplementary material, which is available to authorized users.

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Understanding the function of bacterial and eukaryotic thiolases II by integrating evolutionary and functional approaches

Cited by 24 publications

References 44 publications

Metagenomic Analysis of Cecal Microbiome Identified Microbiota and Functional Capacities Associated with Feed Efficiency in Landrace Finishing Pigs

Metagenomic Analysis of Cecal Microbiome Identified Microbiota and Functional Capacities Associated with Feed Efficiency in Landrace Finishing Pigs

Understanding the intracellular-to-extracellular localization switch of polyhydroxybutyrate polymerase in pseudomonas backgrounds as a microevolutionary process

Functional characterization of thiolase-encoding genes from Xanthophyllomyces dendrorhous and their effects on carotenoid synthesis

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