LINKAGE OF POLYNUCLEOTIDES THROUGH PHOSPHODIESTER BONDS BY AN ENZYME FROM ESCHERICHIA COLI
LINKAGE OF POLYNUCLEOTIDES THROUGH PHOSPHODIESTER BONDS BY AN ENZYME FROM ESCHERICHIA COLI
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DOI：
10.1073/pnas.57.5.1426
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发表时间：
1967-01-01
影响因子：
11.1
通讯作者：
LEHMAN, IR
中科院分区：
文献类型：
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作者：
OLIVERA, BM;LEHMAN, IR
从大肠杆菌的提取物中纯化了约600倍的酶。大肠杆菌，催化短（150个残基）聚脱氧胸苷酸链缩合形成脱氧胸苷酸聚合物，其长度通过形成典型的3“5[image]磷酸二酯键而增加多达20倍。为了使反应发生，酶需要二价阳离子（Mg++或Ca++）;存在于煮沸的E.大肠杆菌;和通过H2键将聚脱氧胸苷酸链固定到长（3000个残基）脱氧腺苷酸聚合物上。这种酶催化噬菌体X DNA的“H2-键合环”形成“共价环”。
An enzyme purified approximately 600-fold from extracts of E. coli, catalyzes the condensation of short (150 residues) polydeoxythmidylate chains to form deoxythymidylate polymers whose length was increased as much as 20-fold by the formation of typical 3''5[image] phosphodiester linkages. For the reaction to occur, the enzyme requires a divalent cation (Mg++ or Ca++); a factor or factors present in boiled extracts of E. coli; and fixation of the polydeoxythymidylate chains by H2 bonds to a long (3000 residues) deoxyadenylate polymer. The enzyme catalyzes the formation of "covalent circles'' from "H2-bonded circles" of phage X DNA.