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噬菌体φX174基因A蛋白与DNA复合物中的键是酪氨酰-5'-磷酸酯。

The bond in the bacteriophage phi X174 gene A protein--DNA complex is a tyrosyl-5'-phosphate ester.

作者信息

van Mansfeld A D, van Teeffelen H A, Baas P D, Veeneman G H, van Boom J H, Jansz H S

出版信息

FEBS Lett. 1984 Aug 6;173(2):351-6. doi: 10.1016/0014-5793(84)80804-2.

Abstract

The bacteriophage phi X174 gene A protein cleaves the viral strand of the double-stranded replicative form (RF) DNA of the phage at a specific site, the origin. It leaves a free 3'-OH at nucleotide 4305 (G) of the phi X DNA sequence and binds covalently to the DNA. The nature and position of the covalent bond have been determined using the octadecadesoxyribonucleotide CAACTTG[32P]ATATTAATAAC. This octadecamer, which corresponds to nucleotides 4299-4316 of phi X viral DNA, is cleaved by gene A protein. Gene A protein is bound to the labelled phosphate via a tyrosyl residue, indicating that binding occurs to the nucleotide corresponding to 4306 (A) of the phi X viral DNA strand.

摘要

噬菌体φX174基因A蛋白在特定位点(即复制起点)切割噬菌体双链复制型(RF)DNA的病毒链。它在φX DNA序列的核苷酸4305(G)处留下一个游离的3'-OH,并与DNA共价结合。共价键的性质和位置已通过十八聚脱氧核糖核苷酸CAACTTG[32P]ATATTAATAAC确定。这个与φX病毒DNA的核苷酸4299 - 4316相对应的十八聚体被基因A蛋白切割。基因A蛋白通过一个酪氨酰残基与标记的磷酸基团结合,表明结合发生在与φX病毒DNA链的4306(A)相对应的核苷酸上。

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