دورية أكاديمية
Structural Dynamics of the Bacillus subtilis MntR Transcription Factor Is Locked by Mn 2+ Binding.
| العنوان: | Structural Dynamics of the Bacillus subtilis MntR Transcription Factor Is Locked by Mn 2+ Binding. |
|---|---|
| المؤلفون: | Jelić Matošević, Zoe, Radman, Katarina, Loubser, Jolene, Crnolatac, Ivo, Piantanida, Ivo, Cukrowski, Ignacy, Ašler, Ivana Leščić, Bertoša, Branimir |
| المصدر: | International Journal of Molecular Sciences; Jan2023, Vol. 24 Issue 2, p957, 21p |
| مصطلحات موضوعية: | STRUCTURAL dynamics, TRANSCRIPTION factors, BACILLUS (Bacteria), MOLECULAR dynamics, DIFFERENTIAL scanning calorimetry |
| مستخلص: | Manganese (II) ions are essential for a variety of bacterial cellular processes. The transcription factor MntR is a metallosensor that regulates Mn2+ ion homeostasis in the bacterium Bacillus subtilis. Its DNA-binding affinity is increased by Mn2+ ion binding, allowing it to act as a transcriptional repressor of manganese import systems. Although experimentally well-researched, the molecular mechanism that regulates this process is still a puzzle. Computational simulations supported by circular dichroism (CD), differential scanning calorimetry (DSC) and native gel electrophoresis (native-PAGE) experiments were employed to study MntR structural and dynamical properties in the presence and absence of Mn2+ ions. The results of molecular dynamics (MD) simulations revealed that Mn2+ ion binding reduces the structural dynamics of the MntR protein and shifts the dynamic equilibrium towards the conformations adequate for DNA binding. Results of CD and DSC measurements support the computational results showing the change in helical content and stability of the MntR protein upon Mn2+ ion binding. Further, MD simulations show that Mn2+ binding induces polarization of the protein electrostatic potential, increasing the positive electrostatic potential of the DNA-binding helices in particular. In order to provide a deeper understanding of the changes in protein structure and dynamics due to Mn2+ binding, a mutant in which Mn2+ binding is mimicked by a cysteine bridge was constructed and also studied computationally and experimentally. [ABSTRACT FROM AUTHOR] |
| Copyright of International Journal of Molecular Sciences is the property of MDPI and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.) | |
| قاعدة البيانات: | Complementary Index |
Full Text Finder كن أول من يترك تعليقا!