Frontiers in Molecular Biosciences (Nov 2022)

The rational design of iron-sulfur cluster binding site for prolonged stability in magnetoreceptor MagR

  • Tianyang Tong,
  • Tianyang Tong,
  • Yajie Zhou,
  • Yajie Zhou,
  • Fan Fei,
  • Fan Fei,
  • Xiujuan Zhou,
  • Xiujuan Zhou,
  • Zhen Guo,
  • Shun Wang,
  • Shun Wang,
  • Jing Zhang,
  • Jing Zhang,
  • Peng Zhang,
  • Peng Zhang,
  • Tiantian Cai,
  • Guohui Li,
  • Yuebin Zhang,
  • Junfeng Wang,
  • Junfeng Wang,
  • Junfeng Wang,
  • Junfeng Wang,
  • Can Xie,
  • Can Xie,
  • Can Xie,
  • Can Xie

DOI
https://doi.org/10.3389/fmolb.2022.1051943
Journal volume & issue
Vol. 9

Abstract

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Iron-sulfur proteins play essential roles in a wide variety of cellular processes such as respiration, photosynthesis, nitrogen fixation and magnetoreception. The stability of iron-sulfur clusters varies significantly between anaerobic and aerobic conditions due to their intrinsic sensitivity to oxygen. Iron-sulfur proteins are well suited to various practical applications as molecular redox sensors or molecular “wires” for electron transfer. Various technologies have been developed recently using one particular iron-sulfur protein, MagR, as a magnetic tag. However, the limited protein stability and low magnetic sensitivity of MagR hindered its wide application. Here in this study, the iron-sulfur binding site of pigeon clMagR was rationally re-designed. One such mutation, T57C in pigeon MagR, showed improved iron-sulfur binding efficiency and higher iron content, as well as prolonged thermostability. Thus, clMagRT57C can serve as a prototype for further design of more stable and sensitive magnetic toolbox for magnetogenetics in the future.

Keywords