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j.bbrc.2012.09.116.pdf | 405.97 kB | Adobe PDF | 見る/開く |
タイトル: | Kinetic analysis of reverse transcriptase activity of bacterial family A DNA polymerases. |
著者: | Yasukawa, Kiyoshi Konishi, Atsushi Shinomura, Mayu Nagaoka, Eriko Fujiwara, Shinsuke |
著者名の別形: | 保川, 清 |
キーワード: | Family A DNA polymerase Moloney murine leukemia virus Reverse transcriptase Template-primer Thermotoga petrophila Thermusthermophilus |
発行日: | 26-Oct-2012 |
出版者: | Elsevier Inc. |
誌名: | Biochemical and biophysical research communications |
巻: | 427 |
号: | 3 |
開始ページ: | 654 |
終了ページ: | 658 |
抄録: | Some bacterial thermostable, wild-type or genetically engineered family A DNA polymerases have reverse transcriptase activity. However, difference in reverse transcriptase activities of family A DNA polymerases and retroviral reverse transcriptases (RTs) is unclear. In this study, comparative kinetic analysis was performed for the reverse transcriptase activities of the wild-type enzyme of family A DNA polymerase (M1pol(WT)) from Thermus thermophilus M1 and the variant enzyme of family A DNA polymerase (K4pol(L329A)), in which the mutation of Leu329→Ala is undertaken, from Thermotoga petrophila K4. In the incorporation of dTTP into poly(rA)-p(dT)(45), the reaction rates of K4pol(L329A) and M1pol(WT) exhibited a saturated profile of the Michaelis-Menten kinetics for dTTP concentrations but a substrate inhibition profile for poly(rA)-p(dT)(45) concentrations. In contrast, the reaction rates of Moloney murine leukemia virus (MMLV) RT exhibited saturated profiles for both dTTP and poly(rA)-p(dT)(45) concentrations. This suggests that high concentrations of DNA-primed RNA template decrease the efficiency of cDNA synthesis with bacterial family A DNA polymerases. |
著作権等: | © 2012 Elsevier Inc. This is not the published version. Please cite only the published version. この論文は出版社版でありません。引用の際には出版社版をご確認ご利用ください。 |
URI: | http://hdl.handle.net/2433/161657 |
DOI(出版社版): | 10.1016/j.bbrc.2012.09.116 |
PubMed ID: | 23026053 |
出現コレクション: | 学術雑誌掲載論文等 |
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