Part:BBa_K1790005:Design

GLN_H gene source

TM

Thermotoga maritima is a hyperthermophilic organism that is a member of the order Thermotogales. Thermotoga maritima is the only bacterium known to grow at this high a temperature; the only other organisms known to live in environments this extreme are members of the domain Archaea First discovered in the sediment of a marine geothermal area near Vulcano, Italy, Thermotoga maritima resides in hot springs as well as hydrothermal vents. The ideal environment for the organism is a water temperature of 80 °C (176 °F), though it is capable of growing in waters of 55–90 °C The genome of T. maritima consists of a single circular 1.8 megabase chromosome encoding for 1877 proteins.

Our biosensor

Our protein

The Gln-H protein after adding the linkers. The linkers added to the ends of the C terminal and N terminal. This mutation cycle allows one of the new Terminal ends of the protein to unite (when on each end is half of another reporter gene), in actual fact the two parts of the gene come together and form comfortable conditions for creating color. The change in color will occur only when the connection is through gluten. The mutation protein will act as follows: Without gluten - the protein will be in the open position and therefore the half enzyme will remain inactive and there will not be a color reaction. The presence of gluten - the protein closes, following; the half enzyme will close and become an active enzyme with the result of a color reaction.

References

Daniel Leffler, MD, MS, The Celiac Center at Beth Israel Deaconness Medical Center Datamonitor Group, 2009, Packaged Facts, 2011 ahttp://www.biocyc.org/ECOLI/NEW-IMAGE?type=GENE&object=G6932

Satoshi Okada et al. (2009) Circular permutation of ligand-binding module improves dynamic range of genetically encoded FRET-based nanosensor. Department of Computational Biology, Graduate School of Frontier Sciences, University of Tokyo, 5-1-5 Kashiwanoha, Kashiwa 277-8561, Japan

Katrin Gruenwald1 et al. (2012) Visualization of Glutamine Transporter Activities in Living Cells Using Genetically Encoded Glutamine Sensors. Department of Plant Pathology, Physiology and Weed Science, Virginia Tech, Blacksburg, Virginia, United States of America, 2 Department of Botany, Faculty of Science, Hamdard University, New Delhi, India

Fabio Cimaglia et al. (2014) Study of a New Gliadin Capture Agent and Development of a Protein Microarray as a New Approach for Gliadin Detection Biotecgen srl, Lecce, Italy 2 Consiglio Nazionale delle Ricerche- Istituto di Scienze delle Produzioni Alimentari, Unità Operativa di Lecce, Lecce, Italy

Ste´phanie Cabantous et al (2013). A New Protein-Protein Interaction Sensor Based on Tripartite Split-GFP Association. INSERM UMR1037, Cancer Research Center of Toulouse, Universite´ de Toulouse, Institut Claudius Regaud, F-31052 Toulouse, France, 2 Bioscience Division, MS-M888, Los Alamos National Laboratory, Los Alamos, NM 87545, USA, 3 CNRS, IPBS (Institut de Pharmacologie et de Biologie Structurale), F-31077 Toulouse, France; Universite´ de Toulouse; UPS, IPBS, F-31077 Toulouse, France, 4 Department of Microbiology, University of Washington, Seattle, WA 98195, USA, 5 Rockefeller University, New York, NY 10065, USA

Alessio Ausili et al (2013). Periplasmic Binding Proteins in Thermophiles: Characterization and Potential Application of an Arginine-Binding Protein from Thermotoga maritima: A Brief Thermo-Story. Laboratory for Molecular Sensing, Institute of Protein Biochemistry, CNR, Via Pietro Castellino, 111, Napoli, 80131, Italy; E-Mails: a.ausili@ibp.cnr.it (A.A.); m.staiano@ibp.cnr.it (M.S.); a.varriale@ibp.cnr.it (A.V.); a.capo@ibp.cnr.it (A.C.) 2 Department of Chemistry, University of Richmond, Richmond, VA 23173, USA; E-Mail: jdattelb@richmond.edu