Thermus aquaticus

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Thermus aquaticus
Scientific classification
Kingdom: Eubacteria Genus: Thermus Species: aquaticus

Description and significance

Thermus Aquaticus isolated in 1969 by brocks and Freee of University of Indiana have proved to be of extreme importance in the field of Microbiology due to it's thermostability. It is a gram negative bacteria both motile (presence of a flagellum) or immotile.

Genome structure

This section discusses the genome structure Thermus Aquaticus contains pillus like structures used in conjugation. 12 genes in 3 loci were found to encode for preplin like proteins essential for natural transfomation. Core enzyme Taq Rna polymerase consists of 4 different subunits: Alpha(2), Beta, Beta prime, and Omega, complexed with Sigma factor. The enzyme is claw shaped with a clamp that closes on an internal channel containing Magnesium ions and the active site. Sigma interacts with core enzyme and specifically binds to promoter to widen the channel allowing DNA into interior of polymerase complex

Cell structure and metabolism

Thermus Aquaticus not only can function at high temperatures but they thrive in higher temperatures. Optimum growth is seen between 60 and 75 degrees celsius (could go as low as 35

degrees celsius to as high as 85 degrees celsius). PH ranges from 7.5 to 8.0 generally but some strains could be between 5.1 to 9.5. This organism is a chemotroph using

carbohyddrates, amino acids, caboxylic acids and peptides for growth. Monosaccharides are generally used for carbons sources but sucrose, maltose(Icelandic stains) and even some

fewer strains use glucose. There is also a variance in the proteins isolated from different strains; Elastin, Fibrin and Casein. Not all strains can hydrolize all substrates.

Membranes of these proteins are remarkably temperature stable and the heat stability of the enzymes and proteins synthesis systems allow them to function efficiently at high 

tempratures. Many factors contribute to the stability of the proteins:

1) Highly organized hydrophobic interiors 2) More hydrogen bonds and presence of other non covalent bonds strengthen the structure. 3) Larger quantities of amino acids like Proline make peptide chain less flexible. 4) Proteins aided and stabilized by special chaperone proteins. 5) Some evidence that DNA is stabilized by histone like proteins. 6) Their membrane lipids tend to be more saturated and more branched and posses higher molecular weight resulting in a higher melting point and in turn more thermostable.