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Sensing domain and extension rate of a family B-type DNA polymerase determine the stalling at a deaminated base
- Authors
- Kim, Y.J.[Kim, Y.J.]; Cha, S.-S.[ Cha, S.-S.]; Lee, H.S.[ Lee, H.S.]; Ryu, Y.G.[ Ryu, Y.G.]; Bae, S.S.[ Bae, S.S.]; Cho, Y.[ Cho, Y.]; Cho, H.-S.[ Cho, H.-S.]; Kim, S.-J.[ Kim, S.-J.]; Kwon, S.-T.[Kwon, S.-T.]; Lee, J.-H.[ Lee, J.-H.]; Kang, S.G.[ Kang, S.G.]
- Issue Date
- 2008
- Keywords
- Archaeal family B-type DNA polymerase; Extension rate; Hypoxanthine; TNA1 DNA polymerase; Uracil sensing
- Citation
- Journal of Microbiology and Biotechnology, v.18, no.8, pp.1377 - 1385
- Indexed
- SCOPUS
KCI
- Journal Title
- Journal of Microbiology and Biotechnology
- Volume
- 18
- Number
- 8
- Start Page
- 1377
- End Page
- 1385
- ISSN
- 1017-7825
- Abstract
- The uracil-sensing domain in archaeal family B-type DNA polymerases recognizes pro-mutagenic uracils in the DNA template, leading to stalling of DNA polymerases. Here, we describe our new findings regarding the molecular mechanism underpinning the stalling of polymerases. We observed that two successive deaminated bases were required to stall TNA1 and KOD1 DNA polymerases, whereas a single deaminated base was enough for stalling Pfu DNA polymerase, in spite of the virtually identical uracil-sensing domains. TNA1 and KOD1 DNA polymerases have a much higher extension rate than Pfu DNA polymerase; decreasing the extension rate resulted in stalling by TNA1 and KOD1 DNA polymerases at a single deaminated base. These results strongly suggest that these polymerases require two factors to stop DNA polymerization at a single deaminated base: the presence of the uracil-sensing domain and a relatively slow extension rate. © The Korean Society for Microbiology and Biotechnology.
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