Improvement of the 3'-5' exonuclease activity of Taq DNA polymerase by protein engineering in the active site

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dc.contributor.authorYoung Hyun Park-
dc.contributor.authorHye Ja Choi-
dc.contributor.authorDae Sil Lee-
dc.contributor.authorYoung Soo Kim-
dc.date.accessioned2017-04-19T08:55:31Z-
dc.date.available2017-04-19T08:55:31Z-
dc.date.issued1997-
dc.identifier.issn1016-8478-
dc.identifier.urihttps://oak.kribb.re.kr/handle/201005/4484-
dc.description.abstractTaq DNA polymerase from Thermus aquaticus has been shown to be very useful in the polymerase chain reaction method. Taq DNA polymerase has a domain at its amino terminus (residue 1 to 291) that has a 5′-3′ exonuclease activity, a 3′-5′ exonuclease domain in the middle (residue 292 to 423), and a domain at its C-terminus that catalyzes polymerase reactions. Taq DNA polymerase is classified into the polI family which is represented by E. coli DNA polymerase I. The three dimensional structural alignment of 3′-5′ exonuclease domains from the polI family, DNA polymerases leads us to understand why Taq DNA polymerase does not carry out proof-reading in the polymerase chain reaction. Three sequence motifs, called ExoI, II, and III must be present in order to carry out proof-reading by the 3′-5′ exonuclease reaction in DNA polymerization, but Taq DNA polymerase contains none of them. The key catalytic module in the 3′-5′ exonuclease is two metal ions chelated by active-site carboxylic amino acids. In order to render the 3′-5′ exonuclease activity in Taq DNA polymerase, a catalytic module was constructured in the active site by protein engineering. The mutant Taq DNA polymerase shows twice as much the 3′-5′ exonuclease activity as that of wild-type DNA polymerase.-
dc.publisherKorea Soc-Assoc-Inst-
dc.titleImprovement of the 3'-5' exonuclease activity of Taq DNA polymerase by protein engineering in the active site-
dc.title.alternativeImprovement of the 3'-5' exonuclease activity of Taq DNA polymerase by protein engineering in the active site-
dc.typeArticle-
dc.citation.titleMolecules and Cells-
dc.citation.number3-
dc.citation.endPage424-
dc.citation.startPage419-
dc.citation.volume7-
dc.contributor.affiliatedAuthorDae Sil Lee-
dc.contributor.alternativeName박영현-
dc.contributor.alternativeName최혜자-
dc.contributor.alternativeName이대실-
dc.contributor.alternativeName김영수-
dc.identifier.bibliographicCitationMolecules and Cells, vol. 7, no. 3, pp. 419-424-
dc.description.journalClassY-
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