Bibliographic Details
| Title: |
Definition of the Binding Architecture to a Target Promoter of HP1043, the Essential Master Regulator of Helicobacter pylori. |
| Authors: |
Zannoni, Annamaria1 (AUTHOR) annamaria.zannoni2@unibo.it, Pelliciari, Simone1 (AUTHOR) simone.pelliciari@newcastle.ac.uk, Musiani, Francesco1 (AUTHOR) francesco.musiani@unibo.it, Chiappori, Federica2 (AUTHOR) federica.chiappori@itb.cnr.it, Roncarati, Davide1 (AUTHOR) davide.roncarati@unibo.it, Scarlato, Vincenzo1 (AUTHOR) davide.roncarati@unibo.it |
| Source: |
International Journal of Molecular Sciences. Aug2021, Vol. 22 Issue 15, p7848-7848. 1p. |
| Subject Terms: |
*HELICOBACTER pylori, *MOLECULAR dynamics, *PROTEIN-protein interactions, *DNA-protein interactions, *PHOSPHORYLATION, *RNA polymerases |
| Abstract: |
HP1043 is an essential orphan response regulator of Helicobacter pylori orchestrating multiple crucial cellular processes. Classified as a member of the OmpR/PhoB family of two-component systems, HP1043 exhibits a highly degenerate receiver domain and evolved to function independently of phosphorylation. Here, we investigated the HP1043 binding mode to a target sequence in the hp1227 promoter (Php1227). Scanning mutagenesis of HP1043 DNA-binding domain and consensus sequence led to the identification of residues relevant for the interaction of the protein with a target DNA. These determinants were used as restraints to guide a data-driven protein-DNA docking. Results suggested that, differently from most other response regulators of the same family, HP1043 binds in a head-to-head conformation to the Php1227 target promoter. HP1043 interacts with DNA largely through charged residues and contacts with both major and minor grooves of the DNA are required for a stable binding. Computational alanine scanning on molecular dynamics trajectory was performed to corroborate our findings. Additionally, in vitro transcription assays confirmed that HP1043 positively stimulates the activity of RNA polymerase. [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.) |
| Database: |
Academic Search Complete |
|
Full text is not displayed to guests. |
Login for full access.
|
