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

文献类型：期刊论文

作者Tong, Tianyang8,9; Zhou, Yajie1,2,9; Fei, Fan3,9; Zhou, Xiujuan3,9; Guo, Zhen4; Wang, Shun1,2,9; Zhang, Jing3,9; Zhang, Peng3,9; Cai, Tiantian5; Li, Guohui7
刊名FRONTIERS IN MOLECULAR BIOSCIENCES
出版日期2022-11-10
卷号9
关键词iron-sulfur cluster magnetoreceptor MagR rational design thermostability
DOI10.3389/fmolb.2022.1051943
通讯作者Zhang, Yuebin(zhangyb@dicp.ac.cn) ; Wang, Junfeng(junfeng@hmfl.ac.cn) ; Xie, Can(canxie@hmfl.ac.cn)
英文摘要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, clMagR(T57C) can serve as a prototype for further design of more stable and sensitive magnetic toolbox for magnetogenetics in the future.
WOS关键词ELECTRON-TRANSFER ; ESSENTIAL 2FE-2S ; 4FE-4S CLUSTERS ; PROTEINS ; BIRDS ; EPR
资助项目Presidential Foundation of Hefei Institutes of Physical Science ; Chinese Academy of Sciences ; National Natural Science Foundation of China ; [31640001]
WOS研究方向Biochemistry & Molecular Biology
语种英语
出版者FRONTIERS MEDIA SA
WOS记录号WOS:000890686500001
资助机构Presidential Foundation of Hefei Institutes of Physical Science ; Chinese Academy of Sciences ; National Natural Science Foundation of China
源URL[http://ir.hfcas.ac.cn:8080/handle/334002/131697]  
专题中国科学院合肥物质科学研究院
通讯作者Zhang, Yuebin; Wang, Junfeng; Xie, Can
作者单位1.Anhui Univ, Inst Phys Sci, Hefei, Anhui, Peoples R China
2.Anhui Univ, Inst Informat Technol, Hefei, Anhui, Peoples R China
3.Univ Sci & Technol China, Sci Isl Branch Grad Sch, Hefei, Anhui, Peoples R China
4.Peking Univ, Sch Life Sci, Beijing, Peoples R China
5.Harvard Med Sch, Dept Biol Chem & Mol Pharmacol, Boston, MA USA
6.Int Magnetobiol Frontier Res Ctr, Sci Isl, Hefei, Peoples R China
7.Chinese Acad Sci, Dalian Inst Chem Phys, State Key Lab Mol React Dynam, Dalian, Peoples R China
8.Anhui Med Univ, Sch Basic Med, Dept Anat, Hefei, Anhui, Peoples R China
9.Hefei Inst Phys Sci, Chinese Acad Sci, High Magnet Field Lab, Sci Isl, Hefei, Peoples R China
推荐引用方式
GB/T 7714		 Tong, Tianyang,Zhou, Yajie,Fei, Fan,et al. The rational design of iron-sulfur cluster binding site for prolonged stability in magnetoreceptor MagR[J]. FRONTIERS IN MOLECULAR BIOSCIENCES,2022,9.
APA Tong, Tianyang.,Zhou, Yajie.,Fei, Fan.,Zhou, Xiujuan.,Guo, Zhen.,...&Xie, Can.(2022).The rational design of iron-sulfur cluster binding site for prolonged stability in magnetoreceptor MagR.FRONTIERS IN MOLECULAR BIOSCIENCES,9.
MLA Tong, Tianyang,et al."The rational design of iron-sulfur cluster binding site for prolonged stability in magnetoreceptor MagR".FRONTIERS IN MOLECULAR BIOSCIENCES 9(2022).

入库方式： OAI收割

来源：合肥物质科学研究院

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