family B-type DNA polymerase의 탈아미노산 된 염기의 sensing 기작연구

DC Field Value Language
dc.contributor.author 김윤재 -
dc.contributor.author 차선신 -
dc.contributor.author 이현숙 -
dc.contributor.author 유용구 -
dc.contributor.author 배승섭 -
dc.contributor.author 조요나 -
dc.contributor.author 조현수 -
dc.contributor.author 김상진 -
dc.contributor.author 권석태 -
dc.contributor.author 이정현 -
dc.contributor.author 강성균 -
dc.date.accessioned 2020-07-17T00:50:27Z -
dc.date.available 2020-07-17T00:50:27Z -
dc.date.created 2020-02-11 -
dc.date.issued 2008-09-01 -
dc.identifier.uri https://sciwatch.kiost.ac.kr/handle/2020.kiost/29828 -
dc.description.abstract The uracil-sensing domain in archaeal family B-type DNA polymerases recognizes the pro-mutagenic uracil in the DNA template, which leads to the stalling of DNA polymerases. Here, we describe our new findings regarding the recognition spectrum of the uracil-sensing domain of family B-type DNA polymerases, the molecular mechanism underpinning the stalling of polymerases, and a method to increase the efficiency of PCR amplification. The uracil-sensing domain of Pfu DNA polymerase appears to recognize hypoxanthine as well as uracil, as confirmed by primer extension assay, mutation study and molecular docking. Interestingly, we observed that two successive deaminated bases were required to stall TNA1 and KOD DNA polymerases while a single deaminated base was enough for stalling Pfu polymerase in spite of the virtually identical uracil-sensing domain. The facts that TNA1 and KOD DNA polymerases retain much higher extension rates than Pfu DNA polymerase and decrease of extension rate resulted in stalling TNA1 and KOD DNA polymerases at a single deaminated base, strongly suggest that the stalling is determined by the extension rate of DNA polymerases along with possessing uracil-sensing domain. It was demonstrated that dITP is spontaneously generated during PCR amplification and dITPase activity of HAM1-like protein from Thermococcus onnurineus NA1 enhances the PCR amplification yield of TNA1 and Pfu DNA polymerases. -
dc.description.uri 1 -
dc.language English -
dc.publisher International Society of Extremophile -
dc.relation.isPartOf Extremophiles 2008 -
dc.title family B-type DNA polymerase의 탈아미노산 된 염기의 sensing 기작연구 -
dc.title.alternative Sensing domain and extension rate of a family B-type DNA polymerase determine the stalling at a deaminated base -
dc.type Conference -
dc.citation.endPage 21 -
dc.citation.startPage 216 -
dc.citation.title Extremophiles 2008 -
dc.contributor.alternativeName 김윤재 -
dc.contributor.alternativeName 차선신 -
dc.contributor.alternativeName 이현숙 -
dc.contributor.alternativeName 배승섭 -
dc.contributor.alternativeName 김상진 -
dc.contributor.alternativeName 이정현 -
dc.contributor.alternativeName 강성균 -
dc.identifier.bibliographicCitation Extremophiles 2008, pp.216 - 21 -
dc.description.journalClass 1 -
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