Transcriptome and proteome profiling of colon mucosa from quercetin fed F344 rats point to tumor preventive mechanisms, increased mitochondrial fatty acid degradation and decreased glycolysis

PROTEOMICS ◽  
2008 ◽  
Vol 8 (1) ◽  
pp. 45-61 ◽  
Author(s):  
Ashwin A. Dihal ◽  
Hester van der Woude ◽  
Peter J. M. Hendriksen ◽  
Halima Charif ◽  
Lennard J. Dekker ◽  
...  
Keyword(s):  
Fatty Acid ◽  
Colon Mucosa ◽  
Fatty Acid Degradation ◽  
Proteome Profiling ◽  
Acid Degradation ◽  
Mitochondrial Fatty Acid ◽  
F344 Rats

scholarly journals Engineering the Monomer Composition of Polyhydroxyalkanoates Synthesized in Saccharomyces cerevisiae

2006 ◽  
Vol 72 (1) ◽  
pp. 536-543 ◽  
Author(s):  
Bo Zhang ◽  
Ross Carlson ◽  
Friedrich Srienc
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Fatty Acid ◽  
Chain Length ◽  
Fatty Acid Metabolism ◽  
Acid Metabolism ◽  
Pha Synthase ◽  
Fatty Acid Degradation ◽  
Medium Chain ◽  
Acid Degradation ◽  
Wide Range

ABSTRACT Polyhydroxyalkanoates (PHAs) have received considerable interest as renewable-resource-based, biodegradable, and biocompatible plastics with a wide range of potential applications. We have engineered the synthesis of PHA polymers composed of monomers ranging from 4 to 14 carbon atoms in either the cytosol or the peroxisome of Saccharomyces cerevisiae by harnessing intermediates of fatty acid metabolism. Cytosolic PHA production was supported by establishing in the cytosol critical β-oxidation chemistries which are found natively in peroxisomes. This platform was utilized to supply medium-chain (C6 to C14) PHA precursors from both fatty acid degradation and synthesis to a cytosolically expressed medium-chain-length (mcl) polymerase from Pseudomonas oleovorans. Synthesis of short-chain-length PHAs (scl-PHAs) was established in the peroxisome of a wild-type yeast strain by targeting the Ralstonia eutropha scl polymerase to the peroxisome. This strain, harboring a peroxisomally targeted scl-PHA synthase, accumulated PHA up to approximately 7% of its cell dry weight. These results indicate (i) that S. cerevisiae expressing a cytosolic mcl-PHA polymerase or a peroxisomal scl-PHA synthase can use the 3-hydroxyacyl coenzyme A intermediates from fatty acid metabolism to synthesize PHAs and (ii) that fatty acid degradation is also possible in the cytosol as β-oxidation might not be confined only to the peroxisomes. Polymers of even-numbered, odd-numbered, or a combination of even- and odd-numbered monomers can be controlled by feeding the appropriate substrates. This ability should permit the rational design and synthesis of polymers with desired material properties.

TetR-family transcriptional repressor Thermus thermophilus FadR controls fatty acid degradation

Microbiology ◽  
2011 ◽  
Vol 157 (6) ◽  
pp. 1589-1601 ◽  
Author(s):  
Yoshihiro Agari ◽  
Kazuko Agari ◽  
Keiko Sakamoto ◽  
Seiki Kuramitsu ◽  
Akeo Shinkai
Keyword(s):  
Fatty Acids ◽  
Fatty Acid ◽  
Target Genes ◽  
Thermus Thermophilus ◽  
Acyl Chain ◽  
Metabolic Energy ◽  
Straight Chain ◽  
Fatty Acid Degradation ◽  
Acid Degradation

In the extremely thermophilic bacterium Thermus thermophilus HB8, one of the four TetR-family transcriptional regulators, which we named T. thermophilus FadR, negatively regulated the expression of several genes, including those involved in fatty acid degradation, both in vivo and in vitro. T. thermophilus FadR repressed the expression of the target genes by binding pseudopalindromic sequences covering the predicted −10 hexamers of their promoters, and medium-to-long straight-chain (C10–18) fatty acyl-CoA molecules were effective for transcriptional derepression. An X-ray crystal structure analysis revealed that T. thermophilus FadR bound one lauroyl (C12)-CoA molecule per FadR monomer, with its acyl chain moiety in the centre of the FadR molecule, enclosed within a tunnel-like substrate-binding pocket surrounded by hydrophobic residues, and the CoA moiety interacting with basic residues on the protein surface. The growth of T. thermophilus HB8, with palmitic acid as the sole carbon source, increased the expression of FadR-regulated genes. These results indicate that in T. thermophilus HB8, medium-to-long straight-chain fatty acids can be used for metabolic energy under the control of FadR, although the major fatty acids found in this strain are iso- and anteiso-branched-chain (C15 and 17) fatty acids.

scholarly journals Long Chain Fatty Acid Degradation Coupled to Biological Sulfidogenesis: A Prospect for Enhanced Metal Recovery

2020 ◽  
Vol 8 ◽  
Author(s):  
Anna Patrícya Florentino ◽  
Rachel Biancalana Costa ◽  
Yuansheng Hu ◽  
Vincent O'Flaherty ◽  
Piet N. L. Lens
Keyword(s):  
Fatty Acid ◽  
Metal Recovery ◽  
Chain Fatty Acid ◽  
Long Chain Fatty Acid ◽  
Fatty Acid Degradation ◽  
Acid Degradation ◽  
Long Chain

Effect of staging on volatile fatty acid degradation in a sulfidogenic granular sludge reactor

1998 ◽  
Vol 32 (4) ◽  
pp. 1178-1192 ◽  
Author(s):  
P.N.L. Lens ◽  
M.C. Van den Bosch ◽  
L.W. Hulshoff Pol ◽  
G. Lettinga
Keyword(s):  
Fatty Acid ◽  
Volatile Fatty Acid ◽  
Granular Sludge ◽  
Fatty Acid Degradation ◽  
Acid Degradation

scholarly journals Identification and characterization of an acyl-CoA dehydrogenase from Pseudomonas putida KT2440 that shows preference towards medium to long chain length fatty acids

Microbiology ◽  
2014 ◽  
Vol 160 (8) ◽  
pp. 1760-1771 ◽  
Author(s):  
Maciej W. Guzik ◽  
Tanja Narancic ◽  
Tatjana Ilic-Tomic ◽  
Sandra Vojnovic ◽  
Shane T. Kenny ◽  
...  
Keyword(s):  
Fatty Acids ◽  
Fatty Acid ◽  
Pseudomonas Putida ◽  
Chain Length ◽  
Recombinant Expression ◽  
Nutrient Utilization ◽  
Ecological Niches ◽  
Fatty Acid Degradation ◽  
Acid Degradation

Diverse and elaborate pathways for nutrient utilization, as well as mechanisms to combat unfavourable nutrient conditions make Pseudomonas putida KT2440 a versatile micro-organism able to occupy a range of ecological niches. The fatty acid degradation pathway of P. putida is complex and correlated with biopolymer medium chain length polyhydroxyalkanoate (mcl-PHA) biosynthesis. Little is known about the second step of fatty acid degradation (β-oxidation) in this strain. In silico analysis of its genome sequence revealed 21 putative acyl-CoA dehydrogenases (ACADs), four of which were functionally characterized through mutagenesis studies. Four mutants with insertionally inactivated ACADs (PP_1893, PP_2039, PP_2048 and PP_2437) grew and accumulated mcl-PHA on a range of fatty acids as the sole source of carbon and energy. Their ability to grow and accumulate biopolymer was differentially negatively affected on various fatty acids, in comparison to the wild-type strain. Inactive PP_2437 exhibited a pattern of reduced growth and PHA accumulation when fatty acids with lengths of 10 to 14 carbon chains were used as substrates. Recombinant expression and biochemical characterization of the purified protein allowed functional annotation in P. putida KT2440 as an ACAD showing clear preference for dodecanoyl-CoA ester as a substrate and optimum activity at 30 °C and pH 6.5–7.

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