The taq polymerase enzyme is obtained from
A. ThiobaciLLus ferrooxidans
B. Bacillus subtilis
C. Pseudomonas putida
D. Thermus aquaticus
Answer
584.1k+ views
Hint: To solve this question, we must first understand the concept of Taq Polymerase enzyme. Then we need to assess the process of its formation and then only we can conclude the correct answer.
Complete answer:
Before we move forward with the solution of this given question, let us first understand some basic concepts:
Taq Polymerase:
1. It is a thermostable DNA polymerase named after the thermophilic bacterium Thermus aquaticus from which it was originally isolated by Chien et al. in \[1976\]. Its name is often abbreviated to Taq Pol or simply Taq. It is frequently used in the polymerase chain reaction (PCR), a method for greatly amplifying the quantity of short segments of DNA.
2. Thermus aquaticus is a bacterium that lives in hot springs and hydrothermal vents, and Taq polymerase was identified as an enzyme able to withstand the protein-denaturing conditions (high temperature) required during PCR. Therefore, it replaced the DNA polymerase from E. coli originally used in PCR.
3. Some thermostable DNA polymerases have been isolated from other thermophilic bacteria and archaea, such as Pfu DNA polymerase, possessing a proofreading activity, and are being used instead of (or in combination with) Taq for high-fidelity amplification. Fidelity can vary much between Taq's, having profound effects in downstream sequencing applications.
So, from the above explanation (first point) we can conclude that taq polymerase enzyme is obtained from Thermus aquaticus.
So, clearly we can conclude that the correct answer is, ‘D. Thermus aquaticus’
Note: Taq polymerase is bound at its polymerase active-site cleft with the blunt end of duplex DNA. As the Taq polymerase is in contact with the bound DNA, its side chains form hydrogen bonds with the purines and pyrimidines of the DNA. The same region of Taq polymerase that has bonded to DNA also binds with exonuclease. These structures bound to the Taq polymerase have different interactions.
Complete answer:
Before we move forward with the solution of this given question, let us first understand some basic concepts:
Taq Polymerase:
1. It is a thermostable DNA polymerase named after the thermophilic bacterium Thermus aquaticus from which it was originally isolated by Chien et al. in \[1976\]. Its name is often abbreviated to Taq Pol or simply Taq. It is frequently used in the polymerase chain reaction (PCR), a method for greatly amplifying the quantity of short segments of DNA.
2. Thermus aquaticus is a bacterium that lives in hot springs and hydrothermal vents, and Taq polymerase was identified as an enzyme able to withstand the protein-denaturing conditions (high temperature) required during PCR. Therefore, it replaced the DNA polymerase from E. coli originally used in PCR.
3. Some thermostable DNA polymerases have been isolated from other thermophilic bacteria and archaea, such as Pfu DNA polymerase, possessing a proofreading activity, and are being used instead of (or in combination with) Taq for high-fidelity amplification. Fidelity can vary much between Taq's, having profound effects in downstream sequencing applications.
So, from the above explanation (first point) we can conclude that taq polymerase enzyme is obtained from Thermus aquaticus.
So, clearly we can conclude that the correct answer is, ‘D. Thermus aquaticus’
Note: Taq polymerase is bound at its polymerase active-site cleft with the blunt end of duplex DNA. As the Taq polymerase is in contact with the bound DNA, its side chains form hydrogen bonds with the purines and pyrimidines of the DNA. The same region of Taq polymerase that has bonded to DNA also binds with exonuclease. These structures bound to the Taq polymerase have different interactions.
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