DC Field | Value | Language |
---|---|---|
dc.contributor.author | Young Hyun Park | - |
dc.contributor.author | Hye Ja Choi | - |
dc.contributor.author | Dae Sil Lee | - |
dc.contributor.author | Young Soo Kim | - |
dc.date.accessioned | 2017-04-19T08:55:31Z | - |
dc.date.available | 2017-04-19T08:55:31Z | - |
dc.date.issued | 1997 | - |
dc.identifier.issn | 1016-8478 | - |
dc.identifier.uri | https://oak.kribb.re.kr/handle/201005/4484 | - |
dc.description.abstract | Taq 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.publisher | Korea Soc-Assoc-Inst | - |
dc.title | Improvement of the 3'-5' exonuclease activity of Taq DNA polymerase by protein engineering in the active site | - |
dc.title.alternative | Improvement of the 3'-5' exonuclease activity of Taq DNA polymerase by protein engineering in the active site | - |
dc.type | Article | - |
dc.citation.title | Molecules and Cells | - |
dc.citation.number | 3 | - |
dc.citation.endPage | 424 | - |
dc.citation.startPage | 419 | - |
dc.citation.volume | 7 | - |
dc.contributor.affiliatedAuthor | Dae Sil Lee | - |
dc.contributor.alternativeName | 박영현 | - |
dc.contributor.alternativeName | 최혜자 | - |
dc.contributor.alternativeName | 이대실 | - |
dc.contributor.alternativeName | 김영수 | - |
dc.identifier.bibliographicCitation | Molecules and Cells, vol. 7, no. 3, pp. 419-424 | - |
dc.description.journalClass | Y | - |
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