Lac抑制因子
DNA
离解(化学)
抑制因子
序列(生物学)
动力学
DNA测序
计算生物学
离解率
生物
遗传学
血浆蛋白结合
生物物理学
化学
基因
细胞生物学
物理
转录因子
物理化学
量子力学
作者
Emil Marklund,Guanzhong Mao,Jinwen Yuan,Spartak Zikrin,Eldar Abdurakhmanov,Sebastian Deindl,Johan Elf
出处
期刊:Science
[American Association for the Advancement of Science (AAAS)]
日期:2022-01-28
卷期号:375 (6579): 442-445
被引量:22
标识
DOI:10.1126/science.abg7427
摘要
Sequence-specific binding of proteins to DNA is essential for accessing genetic information. We derive a model that predicts an anticorrelation between the macroscopic association and dissociation rates of DNA binding proteins. We tested the model for thousands of different lac operator sequences with a protein binding microarray and by observing kinetics for individual lac repressor molecules in single-molecule experiments. We found that sequence specificity is mainly governed by the efficiency with which the protein recognizes different targets. The variation in probability of recognizing different targets is at least 1.7 times as large as the variation in microscopic dissociation rates. Modulating the rate of binding instead of the rate of dissociation effectively reduces the risk of the protein being retained on nontarget sequences while searching.
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