Part:BBa_K1790004:Design
GLN_H gene source
GBS
Geobacillus stearothermophilus (formally Bacillus stearothermophilus) is a rod-shaped, Gram-positive bacterium and a member of the division Firmicutes. The bacteria is a thermophile and is widely distributed in soil, hot springs, ocean sediment, and is a cause of spoilage in food products. It will grow within a temperature range of 30-75 degrees Celsius. Some strains are capable of oxidizing carbon monoxide aerobically. It is commonly used as a challenge organism for sterilization validation studies and periodic check of sterilization cycles. It was first described in 1920 as Bacillus stearothermophilus, but, together with Bacillus thermoglucosidasius, it was reclassified as a member of the genus Geobacillus in 2001. Recently, a DNA polymerase derived from these bacteria, Bst polymerase, has become important in molecular biology applications. Bst polymerase has a helicase-like activity, making it able to unwind DNA strands. Its optimum functional temperature is between 60 and 65 °C and it is denatured at temperatures above 70 °C.
Our biosensor
Our protein
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