Thermotoga Maritima
Thermotoga Maritima - Related Videos
09:11
Screening for Thermotoga maritima Membrane-Bound Pyrophosphatase Inhibitors
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Cited by 6 •
2019
Here we present a screening method for membrane-bound pyrophosphatase (from Thermotoga maritima) inhibitors based on the molybdenum blue reaction in a 96 well plate format.
11:27
X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050
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Cited by 1 •
2020
This protocol has been developed to study the dimer-dodecamer transition of TmPep1050, an M42 aminopeptidase, at the structural level. It is a straightforward pipeline starting from protein purification to X-ray data processing. Crystallogenesis, data set indexation, and molecular replacement have been emphasized through a case of study, TmPep1050H60A H307A variant.
03:47
Screening Inhibitors of Bacterial Membrane-Bound Pyrophosphatase Using a Colorimetric Assay
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2025
Source: Vidilaseris, K., et al. Screening for Thermotoga maritima Membrane-Bound Pyrophosphatase Inhibitors. J. Vis. Exp. (2019)This video demonstrates a colorimetric assay to screen inhibitors of bacterial membrane-bound pyrophosphatase (mPPase) by quantifying orthophosphate release. The method enables identification of compounds that inhibit mPPase from Thermotoga maritima, a potential antimicrobial drug target.
FAQs
Its enzymes remain stable under conditions that would challenge many proteins, making them useful for examining protein structure and function in a high-temperature setting. This stability also supports research into molecular evolution and industrial biocatalysis, where enzyme performance under demanding conditions can be important.
Thermotoga maritima generates energy by fermenting organic compounds without using oxygen. This metabolic strategy connects the organism’s energy production to the availability of suitable organic substrates rather than oxygen, helping researchers examine how anaerobic microorganisms obtain energy in hot marine environments and other oxygen-limited settings.
Its compact, extensively studied genome provides a framework for examining genome organization and horizontal gene transfer, the movement of genetic material between organisms. These features help researchers investigate how microbial genomes change and how organisms acquire or organize genetic information while adapting to extreme environments.
The organism offers a biological model for considering how microorganisms might adapt to environments resembling conditions on early Earth. Its combination of high-temperature growth, anaerobic metabolism, and marine association allows studies of how extreme physical and chemical conditions may have shaped microbial life and its evolutionary history.
Culturing this bacterium requires attention to its characteristic growth conditions: temperatures near 80°C, an anaerobic environment, and access to organic compounds that can be fermented. Maintaining these factors is essential for investigating its metabolism and for obtaining biological material suited to studies of its enzymes, genome, or cellular features.
Researchers may select this organism when they need to investigate enzymes that tolerate high temperatures. Its heat-stable enzymes provide a basis for studying biocatalytic activity under demanding thermal conditions, while also connecting industrial enzyme research with questions about protein structure, stability, and the evolutionary adaptations of microorganisms from extreme habitats.
The distinctive outer sheath, called a toga, provides a recognizable structural feature for investigating how this bacterium is organized at the cell boundary. Although the overview identifies the sheath primarily as a distinguishing trait, its presence also helps researchers distinguish this model organism when examining microbial form alongside its physiology, genome, and evolution.