Version 1
: Received: 3 November 2020 / Approved: 3 November 2020 / Online: 3 November 2020 (12:49:52 CET)
Version 2
: Received: 3 November 2020 / Approved: 4 November 2020 / Online: 4 November 2020 (10:13:32 CET)
Version 3
: Received: 5 November 2020 / Approved: 6 November 2020 / Online: 6 November 2020 (08:51:39 CET)
Version 4
: Received: 9 November 2020 / Approved: 10 November 2020 / Online: 10 November 2020 (12:23:58 CET)
How to cite:
Hamed, M.; Jabour, S. The Role of Divalent Transition Metal Ions in the Binding of Fur Dimer to DNA: Binding of Mn2+ and Co2+ to EC Fur dimer-DNA Complex. Preprints2020, 2020110146. https://doi.org/10.20944/preprints202011.0146.v4
Hamed, M.; Jabour, S. The Role of Divalent Transition Metal Ions in the Binding of Fur Dimer to DNA: Binding of Mn2+ and Co2+ to EC Fur dimer-DNA Complex. Preprints 2020, 2020110146. https://doi.org/10.20944/preprints202011.0146.v4
Hamed, M.; Jabour, S. The Role of Divalent Transition Metal Ions in the Binding of Fur Dimer to DNA: Binding of Mn2+ and Co2+ to EC Fur dimer-DNA Complex. Preprints2020, 2020110146. https://doi.org/10.20944/preprints202011.0146.v4
APA Style
Hamed, M., & Jabour, S. (2020). The Role of Divalent Transition Metal Ions in the Binding of Fur Dimer to DNA: Binding of Mn<sup>2+</sup> and Co<sup>2+</sup> to EC Fur dimer-DNA Complex. Preprints. https://doi.org/10.20944/preprints202011.0146.v4
Chicago/Turabian Style
Hamed, M. and Salih Jabour. 2020 "The Role of Divalent Transition Metal Ions in the Binding of Fur Dimer to DNA: Binding of Mn<sup>2+</sup> and Co<sup>2+</sup> to EC Fur dimer-DNA Complex" Preprints. https://doi.org/10.20944/preprints202011.0146.v4
Abstract
Ferric uptake regulation protein is a repressor protein which binds an AT rich region of DNA (the iron box). Fur binds as a dimer in a helix turn helix mode and it is activated by iron(II) and other divalent transition metal ions at elevated concentrations in a process to regulate the ion uptake. Each transition metal ion induces certain conformational changes to aid the Fur binding, both the N-terminal and C-terminal domains take part in binding to DNA in addition to His 88 and His 86 residues. The process is discussed in view of experimental reports. Fe(II), Mn(II) and Co(II) activate Fur to bind DNA experimentally but Zinc plays a structural role and does not activate Fur to bind DNA.
Keywords
Ferric Uptake Regulation; Fur, Iron(II), Molecular dynamics; DNA; protein
Subject
Biology and Life Sciences, Biochemistry and Molecular Biology
Copyright:
This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
Commenter: Mazen Hamed
Commenter's Conflict of Interests: Author
text editted and improved, Abstract improved