Thermus aquaticus

Thermus aquaticus is a type of gram-negative bacteria known for its ability to withstand high temperatures. Thermus aquaticus is one of several thermophiles in the Deinococcus-Thermus group. Due to this, heat-resistant DNA polymerase Taq has been isolated from it, which is now widely used for polymerase chain reaction and is one of the most important enzymes in molecular biology. This bacterium resides in the hot springs of Yellowstone National Park and other similar regions, including geysers at temperatures above 55 ° C. The bacterium was discovered by Thomas Brock and Hudson Freeze in the Great Fountains of Yellowstone Park.
Contents
1 Biological properties
1.1 Morphology and metabolism
1.2 Genome
2 Thermostable enzymes - 2.1 Aldolase - 2.2 RNA polymerase - 2.3 Taq1-restriction enzyme 2.4 Taq polymerase - 3 Links - Biological properties - Morphology and metabolism
T. aquaticus is a gram-negative rod-shaped bacterium. It does not form capsules and spores, some strains are mobile and have flagella. In the sunlight produces various pigments [1]. Extremely thermophilic chemoorganogeterotroph, an aerobic [2], develops at temperatures above 55 ° C (70 ° C is optimal). Living in hot springs, geysers [3], two strains were isolated from hot tap water [4]. Genome
The genus T. aquaticus of strain HB27 is represented by an annular chromosome of 1894877 base pairs and a megaplasmid pTT27 of 232605 base pairs. The great similarity of the T. aquaticus genomic with the genome of the mesophilic organism Deinococcus radiodurans was noted [5]. Sequencing and analysis of the genome of T. aquaticus of strain Y51MC23, whose chromosome size is 2340768 base pairs, chromosome contains 2570 genes, of which 2520 encode proteins, the content of HC is 68% [6]. T, the aquaticus of strain NTU103 has a plasmid pTA103 with the size of 1965 base pairs, which replicates on a rolling ring principle [7]. T. aquaticus is infected by the bacteriophage IN93, whose genome is represented by a double-stranded ring DNA molecule of 19603 base pairs [8].
Thermostable enzymes
T. aquaticus is an extremely thermophilic bacterium, so its enzymes are thermostable and do not inactivate at elevated temperatures. Some T. aquaticus enzymes (Taq1 restriction enzyme and especially Taq polymerase) have been used extensively as tools for molecular biological and genetic studies [9]. Aldolase
It was initially unclear how T. aquaticus can survive in extreme temperature conditions. , therefore, it was necessary to study T. aquaticus enzymes in detail, in particular how they avoid denaturing at such high temperatures. One of the first T. aquaticus enzymes studied was aldolase [10]. RNA polymerase
The first polymerase isolated from T. aquaticus was RNA polymerase (transcriptase), first obtained in 1974 [11]. Later, crystallographic studies of this enzyme were carried out [12], and then a recombinant RNA polymerase was created from it, intended for molecular biological studies of transcription [13].
Taq1-restrictase
Restriction enzyme Taq1 (Taq1-restrictase) was one of the first T. aquaticus enzymes used for molecular biological studies [14]. Its restriction region is TCGA.
Taq Polymerase
More: Taq Polymerase
Taq Polymerase was first isolated in 1976 [15]. The advantages of this polymerase for biotechnology over the polymerases of other organisms are the ability to work at elevated temperatures (72-80 ° C optimum) and the ability to obtain this polymerase in its pure form. In 1986, Kary Mullis decided to use Taq polymerase for the polymerase chain reaction (PCR) he developed in 1983, given that the polymerase withstood the high (94-96 ° C) temperature required for DNA denaturation. , because of which it was not necessary to introduce a new portion of expensive DNA polymerase after each cycle of amplification. Later, the Taq polymerase gene was cloned and modified to produce a highly efficient commercial product [16]. This polymerase is homologous to the DNA polymerase I (pol I) of Escherichia coli [17]. The Taq polymerase is also restrictedly used in DNA sequencing [18], but due to the large number of polymers [19] (due to the absence of 3'-5 'exonuclease activity), in sequencing and accurate analysis, the Pfu polymerase from the archaea Pyrococcus furiosus [20] is more commonly used (although the AmpliTaqR polymerase has an advantage over the Pfu polymerase because of its higher processivity [21]).
Links
↑ Brock TD, Mercedes RE (1970). Fine Structure of Thermus aquaticus, an Extreme Thermophile. Journal of Bacteriology 104. p. 509—517. PMID 5473907.
↑ Clinton A. Kennedy. The Microbiology of Thermus aquaticus Isolated from Vulcan Hot Springs, Cascade, Idaho. Archive of the original for 2013-06-26.
↑ Brock T. D., Freeze H. (1969). Thermus aquaticus gen. n. and sp. n. and non-sporulating extreme thermophile. Journal of Bacteriology 98. p. 289—297.
↑ Pask-Hughes R, Williams RA (1975). Extremely thermophilic gram-negative bacteria from hot tap water. J Gen Microbiol. 88 (2). with. 321–8. PMID 1097586.
↑ Henne A, Brüggemann H, Raasch C, Wiezer A, Hartsch T, Liesegang H, Johann A, Lienard T, Gohl O, Martinez-Arias R, Jacobi C, Starkuviene V, Schlenczeck S, Dencker S , Huber R, Klenk HP, Kramer W, Merkl R, Gottschalk G, Fritz HJ. The genome sequence of the extreme thermophile Thermus thermophilus. Nat Biotechnol. 22 (5). with. 547–53. PMID 15064768. Unknown parameter ignored | yea = (help)
↑ Thermus aquaticus Y51MC23, unfinished sequence, whole genome shotgun sequencing project NCBI
↑ Chu SF, Shu HY, Lin LC, Chen MY, Tsay SS, Lin GH (2006). Characterization of a rolling-circle replication plasmid from Thermus aquaticus NTU103. Plasmid. 56 (1). with. 46–52. PMID 16675012.
↑ Thermus phage IN93, complete genome of NCBI
↑ http://www.vivo.colostate.edu/hbooks/genetics/biotech/enzymes/hotpolys.html
↑ Freeze H., Brock TD Thermostable Aldolase from Thermus aquaticus // J. Bact. 1970, vol. 101 (2), pp. 541—550
↑ Air G.M., Harris J.I. DNA-Dependent RNA Polymerase From the Thermophilic Bacterium Thermus aquaticus // FEBS Letters 1974, vol. 38 (3), pp. 277—281
↑ http://www.aps.anl.gov/Science/Reports/1999/darsts2.pdf
↑ http://jb.asm.org/cgi/content/abstract/183/ 1/71
↑ Sato S. A single cleavage of Simian virus 40 (SV40) DNA by a site-specific endonuclease from Thermus aquaticus, Taq I // J. Biochem (Tokyo), 1978 83 (2) R. 633
↑ http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pubmed&pubmedid=8432
↑ http://www.ncbi.nlm.nih.gov/pubmed/8324500
↑ http://www.nature.com/nature/journal/v376/n6541/abs/376612a0.html
↑ http://www.pnas.org/content/85/24/9436.abstract
↑ http://findarticles.com/p/articles/mi_qa3874/is_200001/ai_n8886522
↑ http://web.archive.org/web/20071020001733/http://www.sciam.ru/2006/5/ Sciencerf.shtml
↑ http://molbiol.ru/protocol/09_07.html
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Thermus aquaticus

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