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KMID : 1234420100380020158
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Korean Journal of Microbiololgy and Biotechnology
2010 Volume.38 No. 2 p.158 ~ p.162
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Purification and Characterization of the N-terminally Truncated DNA Polymerase from Thermus thermophilus HJ6
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Jeon Seong-Soo
Seo Min-Ho
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Abstract
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The gene encoding Nterminally truncated Tod polymerase (ΔTod polymerase) from Thermus thermophilus HJ6 was expressed in Escherichia coli under the control of the lambda pR and pL tandem promoters on the expression vector pJLA503. The N-terminal domain (250 amino acids) of Tod polymerase was removed without significant effect on enzyme activity and stability, while no 5’→3’ exonuclease activity was detected. The ΔTod polymerase was verified to possess very efficient reverse transcriptase (RT) activity in the presence of MgCl2. The cDNA can also be amplified in the polymerase chain reaction (PCR) with this mutant enzyme. The ΔTod polymerase was exhibited higher activity than the Taq polymerase in a one-step RT-PCR.
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KEYWORD
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DNA polymerase, RT-PCR, Thermus thermophilus, PCR, exonuclease
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