Specificity of protein-DNA interactions in hypersaline environment: structural studies on complexes of Halobacterium salinarum oxidative stress-dependent protein hsRosR

被引：9

作者：

Kutnowski, Nitzan ^{[1
]}

Shmulevich, Fania ^{[1
]}

Davidov, Geula ^{[1
,2
]}

Shahar, Anat ^{[3
]}

Bar-Zvi, Dudy ^{[1
]}

Eichler, Jerry ^{[1
]}

Zarivach, Raz ^{[1
,2
]}

Shaanan, Boaz ^{[1
]}

机构：

[1] Ben Gurion Univ Negev, Dept Life Sci, IL-8410510 Beer Sheva, Israel

[2] Ben Gurion Univ Negev, Natl Inst Biotechnol Negev, IL-8410510 Beer Sheva, Israel

[3] Ben Gurion Univ Negev, Natl Inst Biotechnol Negev, Macromol Crystallog Res Ctr, IL-8410510 Beer Sheva, Israel

来源：

NUCLEIC ACIDS RESEARCH | 2019年 / 47卷 / 16期

基金：

以色列科学基金会;

关键词：

LAMBDA-CI REPRESSOR; ELECTROSTATIC CONTRIBUTIONS; TRANSCRIPTION FACTOR; OPERATOR COMPLEX; BINDING; SALT; ADAPTATION; MECHANISM; WATER; IONS;

D O I：

10.1093/nar/gkz604

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Interactions between proteins and DNA are crucial for all biological systems. Many studies have shown the dependence of protein-DNA interactions on the surrounding salt concentration. How these interactions are maintained in the hypersaline environments that halophiles inhabit remains puzzling. Towards solving this enigma, we identified the DNA motif recognized by the Halobactrium salinarum ROS-dependent transcription factor (hsRosR), determined the structure of several hsRosR-DNA complexes and investigated the DNA-binding process under extreme high-salt conditions. The picture that emerges from this work contributes to our understanding of the principles underlying the interplay between electrostatic interactions and salt-mediated protein-DNA interactions in an ionic environment characterized by molar salt concentrations.

引用

页码：8860 / 8873

页数：14