Untargeted metabolic footprinting reveals a surprising breadth of metabolite uptake and release by Synechococcus sp. PCC 7002.
Summary of "Untargeted metabolic footprinting reveals a surprising breadth of metabolite uptake and release by Synechococcus sp. PCC 7002."
Cyanobacteria are important primary producers in diverse ecosystems, yet little is known about the extent of their metabolic interactions with the environment. We have used an integrated, untargeted metabolic footprinting approach to systematically evaluate the uptake and release of metabolites between a model marine cyanobacterium Synechococcus sp. PCC 7002 and different growth media. It was found that 47 out of 202 detected metabolites were consumed, and an additional 55 metabolites were released by the cells. Surprisingly, Synechococcus was found to uptake a great diversity of metabolites dominant in and specific to its own metabolite extract including histidine betaine (hercynine), γ-glutamyl phenylalanine and a hexosamine-based trisaccharide. This provides Synechococcus a mechanism to benefit from the lysis of part of their population (i.e. due to environmental stress or predation). Additionally, stable isotope probing was used to show that adenine and glutamate are actively metabolized following uptake. A significant turnover of glucosylglycerol, a cyanobacterial compatible solute, as opposed to a negligible turnover of the hexosamine-based trisaccharide were also observed using stable isotope probing. The untargeted metabolic footprinting approach used in this study is generally applicable to investigate metabolic interactions of microorganisms with the environment and may prove useful to construct microbial community foodwebs.
Affiliation
Life Sciences Division, Lawrence Berkeley National Laboratory, 1 Cyclotron Rd, MS 84R0171, Berkeley, California 94720, United States. trnorthen@lbl.gov.
Journal Details
This article was published in the following journal.
Name: Molecular bioSystems
ISSN: 1742-2051
Pages:
Links
- PubMed Source: http://www.ncbi.nlm.nih.gov/pubmed/21935552
- DOI: http://dx.doi.org/10.1039/c1mb05196b
Medical and Biotech [MESH] Definitions
Dna Footprinting
A method for determining the sequence specificity of DNA-binding proteins. DNA footprinting utilizes a DNA damaging agent (either a chemical reagent or a nuclease) which cleaves DNA at every base pair. DNA cleavage is inhibited where the ligand binds to DNA. (from Rieger et al., Glossary of Genetics: Classical and Molecular, 5th ed)
Metabolic Equivalent
A measurement of OXYGEN uptake in a sitting, resting person (resting oxygen consumption), varying with age, sex, race, and other factors. In normal adult men, one MET is approximately 3.5 ml O2/kg/min of body weight. Oxygen uptake during activities or work can be measured in METs which can be use to determine health status and exercise prescription.
Neurotransmitter Uptake Inhibitors
Drugs that inhibit the transport of neurotransmitters into axon terminals or into storage vesicles within terminals. For many transmitters, uptake determines the time course of transmitter action so inhibiting uptake prolongs the activity of the transmitter. Blocking uptake may also deplete available transmitter stores. Many clinically important drugs are uptake inhibitors although the indirect reactions of the brain rather than the acute block of uptake itself is often responsible for the therapeutic effects.
Biotransformation
The chemical alteration of an exogenous substance by or in a biological system. The alteration may inactivate the compound or it may result in the production of an active metabolite of an inactive parent compound. The alterations may be divided into METABOLIC DETOXICATION, PHASE I and METABOLIC DETOXICATION, PHASE II.
Protein Footprinting
A method for determining points of contact between interacting proteins or binding sites of proteins to nucleic acids. Protein footprinting utilizes a protein cutting reagent or protease. Protein cleavage is inhibited where the proteins, or nucleic acids and protein, contact each other. After completion of the cutting reaction, the remaining peptide fragments are analyzed by electrophoresis.
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