|
Hokkaido University Collection of Scholarly and Academic Papers >
Graduate School of Science / Faculty of Science >
Peer-reviewed Journal Articles, etc >
Regulation of the expression of the nickel uptake system in Vibrio cholerae by iron and heme via ferric uptake regulator (Fur)
This item is licensed under:Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International
| Title: | Regulation of the expression of the nickel uptake system in Vibrio cholerae by iron and heme via ferric uptake regulator (Fur) |
| Authors: | Muranishi, Kazuyoshi Browse this author | | Ishimori, Koichiro Browse this author →KAKEN DB | | Uchida, Takeshi Browse this author →KAKEN DB |
| Keywords: | Ferric uptake regulator | | Vibrio cholerae | | nik operon |
| Issue Date: | Mar-2022 |
| Publisher: | Elsevier |
| Journal Title: | Journal of Inorganic Biochemistry |
| Volume: | 228 |
| Start Page: | 111713 |
| Publisher DOI: | 10.1016/j.jinorgbio.2022.111713 |
| Abstract: | Fur (ferric uptake regulator) is a transcription factor that regulates expression of downstream genes containing a specific Fe2+-binding sequence called the Fur box. In Vibrio cholerae, a Fur box is located upstream of the nik operon, which is responsible for nickel uptake, suggesting that its expression is regulated by Fur. However, there are no reports that Ni2+ induces expression of Fur box genes. Accordingly, we here investigated whether Ni2+ or Fe2+ binds to Fur to regulate expression of the nik operon. We found that Fur binds to the Fur box in the presence of Fe2+ with a dissociation constant (Kd) of 1.2 μM, whereas only non-specific binding was observed in the presence of Ni2+. Thus, Fur-mediated expression of the nik operon is dependent on Fe2+, but not Ni2+. Since most iron in cells exists as heme, we examined the effect of heme on the Fur box binding activity of V. cholerae Fur (VcFur). Addition of heme to the VcFur-Fur box complex induced dissociation of VcFur from the Fur box, indicating that expression of the V. cholerae nik operon is regulated by both iron and heme. Furthermore, VCA1098, a nik operon-encoded protein, bound heme with a Kd of 1.3 μM. Collectively, our results suggest that the V. cholerae nik operon is involved not only in nickel uptake but also in heme uptake, and depends on iron and heme concentrations within bacteria. |
| Rights: | ©2022, Elsevier. Licensed under the Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International http://creativecommons.org/licenses/by-nc-nd/4.0/ | | http://creativecommons.org/licenses/by-nc-nd/4.0/ |
| Type: | article (author version) |
| URI: | http://hdl.handle.net/2115/91232 |
| Appears in Collections: | 理学院・理学研究院 (Graduate School of Science / Faculty of Science) > 雑誌発表論文等 (Peer-reviewed Journal Articles, etc)
|
Submitter: 内田 毅
|
