The intracellular localization of glycolate oxidoreductase in <i>Escherichia coli</i>

Sallal, A.-K. J.; Nimer, N. A.

doi:10.1016/0014-5793(89)81673-4

Cited by 13 publications

(7 citation statements)

References 11 publications

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“…Upregulation of genes in a predicted operon coding for lactate uptake and oxidation suggested that the immediate fates of electrons derived from lactate oxidation differ for syntrophic growth and respiratory growth. Notably, the lactate dehydrogenase is homologous to a membrane-bound glycolate oxidase in E. coli that is directly coupled to the electron transport chain (20,26,34). Additionally, the coo genes are upregulated and encode a protein homologous to those found in other Bacteria and Archaea that function as proton (or sodium)-translocating hydrogenases (8,16,22,35), strongly suggesting that they have a similar electrogenic role in Desulfovibrio.…”

Section: Discussionmentioning

confidence: 99%

The Electron Transfer System of Syntrophically Grown Desulfovibrio vulgaris

et al. 2009

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Interspecies hydrogen transfer between organisms producing and consuming hydrogen promotes the decomposition of organic matter in most anoxic environments. Although syntrophic coupling between hydrogen producers and consumers is a major feature of the carbon cycle, mechanisms for energy recovery at the extremely low free energies of reactions typical of these anaerobic communities have not been established. In this study, comparative transcriptional analysis of a model sulfate-reducing microbe, Desulfovibrio vulgaris Hildenborough, suggested the use of alternative electron transfer systems dependent on growth modality. During syntrophic growth on lactate with a hydrogenotrophic methanogen, numerous genes involved in electron transfer and energy generation were upregulated in D. vulgaris compared with their expression in sulfate-limited monocultures. In particular, genes coding for the putative membrane-bound Coo hydrogenase, two periplasmic hydrogenases (Hyd and Hyn), and the well-characterized high-molecular-weight cytochrome (Hmc) were among the most highly expressed and upregulated genes. Additionally, a predicted operon containing genes involved in lactate transport and oxidation exhibited upregulation, further suggesting an alternative pathway for electrons derived from lactate oxidation during syntrophic growth. Mutations in a subset of genes coding for Coo, Hmc, Hyd, and Hyn impaired or severely limited syntrophic growth but had little effect on growth via sulfate respiration. These results demonstrate that syntrophic growth and sulfate respiration use largely independent energy generation pathways and imply that to understand microbial processes that sustain nutrient cycling, lifestyles not captured in pure culture must be considered.Nutrient cycling on earth is determined primarily by cooperative interactions among microorganisms. The sharing of available energy within communities is particularly important in anaerobic systems, where limited energy is divided among highly specialized and metabolically interdependent populations (36,37,39). In the absence of exogenous electron acceptors such as sulfate and nitrate, the mineralization of organic matter in anoxic environments yields primarily carbon dioxide and methane, and this process is controlled by the synergistic activities of multiple anaerobic microbial populations. To better understand the metabolic basis and ecological significance of these syntrophic associations, we constructed an archetypical "community of two" by pairing Desulfovibrio vulgaris Hildenborough with a hydrogenotrophic methanogen, Methanococcus maripaludis strain S2.

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Section: Discussionmentioning

confidence: 99%

The Electron Transfer System of Syntrophically Grown Desulfovibrio vulgaris

et al. 2009

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“…5). In the case of the A. ambivalens SDH, these modules remained unassembled but for instance, in Thiol:fumarate reductase from M. thermoautotrophicum Marburg (43) and anaerobic sn-glycerol-3-phosphate dehydrogenase and Glicolate oxidase from E. coli (40,41,44,45), two of the modules fused and a single peptide holds the cysteine-motif as well as the iron sulfur clusters. In the case of the Hdr from M. thermoautotrophicum Marburg (46), the flavinic peptide bears additional iron-sulfur clusters while maintaining separated the remaining modules.…”

Section: Alternative Anchormentioning

confidence: 98%

Acidianus ambivalens Complex II Typifies a Novel Family of Succinate Dehydrogenases

Lemos

Gomes

Teixeira

2001

Biochemical and Biophysical Research Communications

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“…To this end, membranes were obtained (28) from glc-deleted strain JA151 transformed with plasmid pTP21, using as a control the same strain transformed with the vector or the wild-type strain MC4100 (Fig. 3C).…”

Section: Resultsmentioning

confidence: 99%

glc locus of Escherichia coli: characterization of genes encoding the subunits of glycolate oxidase and the glc regulator protein

et al. 1996

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The locus glc (min 64.5), associated with the glycolate utilization trait in Escherichia coli, is known to contain glcB, encoding malate synthase G, and the gene(s) needed for glycolate oxidase activity. Subcloning, sequencing, insertion mutagenesis, and expression studies showed five additional genes: glcC and in the other direction glcD, glcE, glcF, and glcG followed by glcB. The gene glcC may encode the glc regulator protein. Consistently a chloramphenicol acetyltransferase insertion mutation abolished both glycolate oxidase and malate synthase G activities. The proteins encoded from glcD and glcE displayed similarity to several flavoenzymes, the one from glcF was found to be similar to iron-sulfur proteins, and that from glcG had no significant similarity to any group of proteins. The insertional mutation by a chloramphenicol acetyltransferase cassette in either glcD, glcE, or glcF abolished glycolate oxidase activity, indicating that presumably these proteins are subunits of this enzyme. No effect on glycolate metabolism was detected by insertional mutation in glcG. Northern (RNA) blot experiments showed constitutive expression of glcC but induced expression for the structural genes and provided no evidence for a single polycistronic transcript.

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The intracellular localization of glycolate oxidoreductase in Escherichia coli

Cited by 13 publications

References 11 publications

The Electron Transfer System of Syntrophically Grown Desulfovibrio vulgaris

The Electron Transfer System of Syntrophically Grown Desulfovibrio vulgaris

Acidianus ambivalens Complex II Typifies a Novel Family of Succinate Dehydrogenases

glc locus of Escherichia coli: characterization of genes encoding the subunits of glycolate oxidase and the glc regulator protein

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