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非底物核苷酸与限制性内切核酸酶的结合：Bam HI与其识别序列相互作用的模型。

Binding of non-substrate nucleotides to a restriction endonuclease: a model for the interaction of bam HI with its recognition sequence.

作者信息

Hinsch B, Mayer H, Kula M R

出版信息

Nucleic Acids Res. 1980 Jun 11;8(11):2547-59. doi: 10.1093/nar/8.11.2547.

DOI:10.1093/nar/8.11.2547
PMID:6160464
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC324101/
Abstract

The kinetic constants of the site-specific endonuclease Bam HI for various substrates were determined and binding of non-substrate nucleotides to the enzyme was studied. Agarose gel assays in combination with an integrated Michaelis-Menten equation were used for the evaluation of data. The turnover number was 2.2 min-1 at 37 degrees C with pJC80 DNA as the substrate. It depends on the conformation and base composition of the substrate. Michaelis constants also depend on substrate conformation. Non-substrate polynucleotides were found to inhibit Bam competitively with KI ranging from 10(-6) to > 10(-3) M depending on base composition, base pairing, and helix conformation. Dinucleotides showed sequence-specific, competitive inhibition with KIs ranging from 10(-5) to > 10(-3) M. Mononucleotides and -nucleosides acted noncompetitively. Binding was influenced by the extent of phosphorylation, but not by the nature of the base. KIs varied between 10(-3) and 10(-2) M. The results are discussed with respect to the recognition requirements of Bam HI.

摘要

测定了位点特异性内切酶Bam HI对各种底物的动力学常数，并研究了非底物核苷酸与该酶的结合。采用琼脂糖凝胶分析结合整合的米氏方程来评估数据。以pJC80 DNA为底物时，在37℃下的周转数为2.2 min-1。它取决于底物的构象和碱基组成。米氏常数也取决于底物构象。发现非底物多核苷酸对Bam具有竞争性抑制作用，抑制常数（KI）范围为10(-6)至>10(-3) M，具体取决于碱基组成、碱基配对和螺旋构象。二核苷酸表现出序列特异性的竞争性抑制作用，抑制常数范围为10(-5)至>10(-3) M。单核苷酸和核苷起非竞争性作用。结合受磷酸化程度的影响，但不受碱基性质的影响。抑制常数在10(-3)至10(-2) M之间变化。针对Bam HI的识别要求对结果进行了讨论。

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本文引用的文献

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HELIX--RANDOM COIL TRANSITIONS IN DNA HOMOPOLYMER PAIRS.DNA同聚物对中的螺旋-无规卷曲转变
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