The Escherichia coli fadK (ydiD) Gene Encodes an Anerobically Regulated Short Chain Acyl-CoA Synthetase

Morgan‐Kiss, Rachael M.; Cronan, John E.

doi:10.1074/jbc.m405233200

Cited by 64 publications

(69 citation statements)

References 36 publications

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“…The His 6 -FadD proteins of E. coli and S. enterica were overexpressed in E. coli BL21(DE3)/pLysS, harboring plasmids pRK34 (29) and pSH53, respectively, using the T7 polymerase-dependent expression system. Cultures (1 liter) were grown in LB broth supplemented with ampicillin and chloramphenicol at 37°C until an optical density of about 0.5 was reached, and then 1 mM isopropyl-␤-D-thiogalactopyranoside was added, followed by incubation for 3 h. The cells were harvested by centrifugation at 4,000 ϫ g for 20 min.…”

Section: Methodsmentioning

confidence: 99%

The β-Oxidation Systems ofEscherichia coliandSalmonella entericaAre Not Functionally Equivalent

Iram¹,

Cronan

2006

J Bacteriol

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Based on its genome sequence, the pathway of ␤-oxidative fatty acid degradation in Salmonella enterica serovar Typhimurium LT2 has been thought to be identical to the well-characterized Escherichia coli K-12 system. We report that wild-type strains of S. enterica grow on decanoic acid, whereas wild-type E. coli strains cannot. Mutant strains (carrying fadR) of both organisms in which the genes of fatty acid degradation (fad) are expressed constitutively are readily isolated. The S. enterica fadR strains grow more rapidly than the wild-type strains on decanoic acid and also grow well on octanoic and hexanoic acids (which do not support growth of wild-type strains). By contrast, E. coli fadR strains grow well on decanoic acid but grow only exceedingly slowly on octanoic acid and fail to grow at all on hexanoic acid. The two wild-type organisms also differed in the ability to grow on oleic acid when FadR was overexpressed. Under these superrepression conditions, E. coli failed to grow, whereas S. enterica grew well. Exchange of the wild-type fadR genes between the two organisms showed this to be a property of S. enterica rather than of the FadR proteins per se. This difference in growth was attributed to S. enterica having higher cytosolic levels of the inducing ligands, long-chain acyl coenzyme As (acyl-CoAs). The most striking results were the differences in the compositions of CoA metabolites of strains grown with octanoic acid or oleic acid. S. enterica cleanly converted all of the acid to acetyl-CoA, whereas E. coli accumulated high levels of intermediate-chain-length products. Exchange of homologous genes between the two organisms showed that the S. enterica FadE and FadBA enzymes were responsible for the greater efficiency of ␤-oxidation relative to that of E. coli.

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Section: Methodsmentioning

confidence: 99%

The β-Oxidation Systems ofEscherichia coliandSalmonella entericaAre Not Functionally Equivalent

Iram¹,

Cronan

2006

J Bacteriol

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“…Short-chain fatty acid CoA ligase, which catalyses the formation of acyl-CoA from a shortchain fatty acid, has a central role in the metabolism, development and pathogenicity of many fungi (Hynes et al, 2006). Fatty acids can serve as sole sources of carbon and energy, whilst acyl-CoAs serve as important intermediates in diverse metabolic functions such as fatty acid transport, oxidative degradation of fatty acids and phospholipid biosynthesis, as well as enzyme activation, cell signalling and transcriptional regulation (Morgan-Kiss & Cronan, 2004). Candida albicans differentially regulates carbon assimilation pathways depending on the stage of infection (Barelle et al, 2006;Lorenz & Fink, 2001).…”

Section: R Peres Da Silva and Othersmentioning

confidence: 99%

Differential gene expression analysis of Paracoccidioides brasiliensis during keratinocyte infection

Silva

Matsumoto

Braz

et al. 2011

Journal of Medical Microbiology

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Paracoccidioides brasiliensis is the agent of paracoccidioidomycosis, one of the most important systemic fungal diseases in Latin America. This initiates in lung tissue and can subsequently disseminate to other tissues. Clinical manifestations range from localized forms to disseminated disease that can progress to lethality, probably depending on the relationships among the virulence of the fungus, the immune response and the ability to interact with the surface structures and invade epithelial cells and mononuclear cells of the host. It is generally regarded as a multifocal disease, with oral lesions as the prominent feature. The aim of this study was to evaluate P. brasiliensis yeast infection in normal oral keratinocytes (NOKs). The differential expression of mRNAs and proteins was also determined when the fungus was placed in contact with the cell in order to characterize differentially expressed genes and proteins during P. brasiliensis infection. After contact with NOKs, the fungus appeared to induce alterations in the cells, which showed cellular extensions and cavitations, probably resulting from changes in the actin cytoskeleton seen at 5 and 8 h after infection. Levels of protein expression were higher after reisolation of the fungus from infected NOK culture compared with culture of the fungus in medium. The analysis identified transcripts related to 19 proteins involved in different biological processes. Transcripts were found with multiple functions including induction of cytokines, protein metabolism, alternative carbon metabolism, zinc transport and the stress response during contact with NOKs. The proteins found suggested that the yeast was in a stress situation, as indicated by the presence of RDS1. Nevertheless, the yeast seemed to be proliferating and metabolically active, as shown by the presence of a proteasome, short-chain acetylator, glucosamine-6-phosphate isomerase and ADP/ATP carrier transcripts. Additionally, metabolic pathways may have been activated in order to eliminate toxic substances from the cell as a zinc transporter was detected, which is a potential target for the development of future drugs. INTRODUCTIONParacoccidioides brasiliensis is a thermodimorphic pathogenic fungus, the aetiological agent of paracoccidioidomycosis (PCM), an endemic disease geographically limited to Latin America and one of the most prevalent human deep systemic mycoses found in Brazil, Colombia and Venezuela (San-Blas et al., 2002). The transition from mycelium at 25 u C to yeast at 37 u C is essential for P. brasiliensis to establish the disease (Franco et al., 1997). P. brasiliensis may be inhaled and, once in the lungs, the fungus initiates a process of morphological transition into the pathogenic yeast form (San-Blas et al., 2002).PCM has a multiplicity of clinical presentations, from cutaneous to systemic forms, and can attack various tissues, especially the lungs (Benard & Franco, 2007). Oral mucosal lesions are commonly multiple, with a granular, mulberry-like surface and microulcerations, and ...

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“…Epitope tagging of CT1087 in C. tepidum. A C. tepidum strain expressing CT1087-His 6 from the native genomic location of CT1087 (strain CT1087-His 6 ::aacC1) was constructed according to the method of Morgan-Kiss and Cronan (36). Two PCR products, each carrying a unique restriction site, were generated by using C. tepidum wild-type genomic DNA as the template with primers CT1087-His-F and CT1087-His-R (see Table S1 in the supplemental material).…”

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confidence: 99%

Functional Analysis of Three Sulfide:Quinone Oxidoreductase Homologs in Chlorobaculum tepidum

2009

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Sulfide:quinone oxidoreductase (SQR) catalyzes sulfide oxidation during sulfide-dependent chemo-and phototrophic growth in bacteria. The green sulfur bacterium Chlorobaculum tepidum (formerly Chlorobium tepidum) can grow on sulfide as the sole electron donor and sulfur source. C. tepidum contains genes encoding three SQR homologs: CT0117, CT0876, and CT1087. This study examined which, if any, of the SQR homologs possess sulfide-dependent ubiquinone reduction activity and are required for growth on sulfide. In contrast to CT0117 and CT0876, transcripts of CT1087 were detected only when cells actively oxidized sulfide. Mutation of CT0117 or CT1087 in C. tepidum decreased SQR activity in membrane fractions, and the CT1087 mutant could not grow with >6 mM sulfide. Mutation of both CT0117 and CT1087 in C. tepidum completely abolished SQR activity, and the double mutant failed to grow with >4 mM sulfide. A C-terminal His 6 -tagged CT1087 protein was membrane localized, as was SQR activity. Epitope-tagged CT1087 was detected only when sulfide was actively consumed by cells. Recombinantly produced CT1087 and CT0117 proteins had SQR activity, while CT0876 did not. In summary, we conclude that, under the conditions tested, both CT0117 and CT1087 function as SQR proteins in C. tepidum. CT0876 may support the growth of C. tepidum at low sulfide concentrations, but no evidence was found for SQR activity associated with this protein.

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The Escherichia coli fadK (ydiD) Gene Encodes an Anerobically Regulated Short Chain Acyl-CoA Synthetase

Cited by 64 publications

References 36 publications

The β-Oxidation Systems ofEscherichia coliandSalmonella entericaAre Not Functionally Equivalent

The β-Oxidation Systems ofEscherichia coliandSalmonella entericaAre Not Functionally Equivalent

Differential gene expression analysis of Paracoccidioides brasiliensis during keratinocyte infection

Functional Analysis of Three Sulfide:Quinone Oxidoreductase Homologs in Chlorobaculum tepidum

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