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Temperature and salt concentration alter base-sequence selectivity of a duplex DNA-binding protein.
Molecular BioSystems Pub Date : 2010-01-01 , DOI: 10.1039/b914828k
Satoru Nagatoishi 1 , Yoshikazu Tanaka , Motonori Kudou , Kouhei Tsumoto
Affiliation  

A structural polymorphism of nucleic acids, which depends on the concentration of cations and the conditions of hydration, are strongly involved with interactions between DNA and proteins. In this paper, we report that different DNA sequences bound to hyperthermostable TATA-box-binding protein (PhoTBP) at different combinations of temperature and salt concentration in in vitro selection experiments. As a result of the interaction of-these selected DNAs with PhoTBP, characteristic changes in the numbers of water molecules and ions occurred under each condition of the selection experiment. This finding could help us to understand the solvent environment-dependent preference for base sequences in protein–DNA interactions.

中文翻译:

温度和盐浓度会改变双链DNA结合蛋白的碱基序列选择性。

取决于阳离子浓度和水合条件的核酸结构多态性与DNA和蛋白质之间的相互作用密切相关。在本文中,我们报告了在体外选择实验中,在不同温度和盐浓度组合下,不同的DNA序列与超热TATA盒结合蛋白(PhoTBP)结合。这些选择的DNA与PhoTBP相互作用的结果是,在选择实验的每种条件下,水分子和离子数量的特征发生了变化。这一发现可以帮助我们了解蛋白质-DNA相互作用中碱基序列对溶剂环境的偏好。
更新日期:2019-11-01
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