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大肠杆菌中碱基类似物2-氨基嘌呤的突变特异性。

Mutational specificity of the base analogue, 2-aminopurine, in Escherichia coli.

作者信息

Persing D H, McGinty L, Adams C W, Fowler R G

出版信息

Mutat Res. 1981 Aug;83(1):25-37. doi: 10.1016/0027-5107(81)90068-3.

Abstract

2-Aminopurine (2-AP) is a base analogue of adenine which mispairs with cytosine and causes base-pair substitutions of the transition type. By analyzing the reversion patterns of defined trpA alleles in Escherichia coli we confirm that 2-AP causes both A:T leads to G:C and G:C leads to A:T transitions with the former induced more frequently than the latter. We also find that 2-AP enhances transversions at 3 sites and frameshift mutations at 1 other site. It is unlikely that 2-AP can cause transversions and frameshifts solely by a mispairing mechanism. However, 2-AP-induced transversion and frameshift mutagenesis was not abolished by the presence of an inactive recA allele, indicating this mutagenic activity is not dependent upon recA-directed misrepair.

摘要

2-氨基嘌呤(2-AP)是腺嘌呤的一种碱基类似物,它与胞嘧啶错配并导致转换类型的碱基对替换。通过分析大肠杆菌中特定trpA等位基因的回复模式,我们证实2-AP会导致A:T到G:C以及G:C到A:T的转换,前者的诱导频率高于后者。我们还发现2-AP会增强3个位点的颠换和另一个位点的移码突变。2-AP不太可能仅通过错配机制导致颠换和移码突变。然而,无活性的recA等位基因的存在并没有消除2-AP诱导的颠换和移码诱变,这表明这种诱变活性不依赖于recA介导的错配修复。

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