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Solution structure of TbCentrin4 from Trypanosoma brucei and its interactions with Ca2+ and other centrins

文献类型：期刊论文

作者Shan, Fangzhen1,2; Ye, Kaiqin3,4; Zhang, Jiahai1,2; Liao, Shanhui1,2; Zhang, Xuecheng5; Xu, Chao1,2; Tu, Xiaoming1,2
刊名BIOCHEMICAL JOURNAL
出版日期2018-12-12
卷号475页码:3763-3778
ISSN号0264-6021
DOI10.1042/BCJ20180752
通讯作者Tu, Xiaoming(xmtu@ustc.edu.cn)
英文摘要Centrin is a conserved calcium-binding protein that plays an important role in diverse cellular biological processes such as ciliogenesis, gene expression, DNA repair and signal transduction. In Trypanosoma brucei, TbCentrin4 is mainly localized in basal bodies and bi-lobe structure, and is involved in the processes coordinating karyokinesis and cytokinesis. In the present study, we solved the solution structure of TbCentrin4 using NMR (nuclear magnetic resonance) spectroscopy. TbCentrin4 contains four EF-hand motifs consisting of eight alpha-helices. Isothermal titration calorimetry experiment showed that TbCentrin4 has a strong Ca2+ binding ability. NMR chemical shift perturbation indicated that TbCentrin4 binds to Ca2+ through its C-terminal domain composed of EF-hand 3 and 4. Meanwhile, we revealed that TbCentrin4 undergoes a conformational change and self-assembly induced by high concentration of Ca2+. Intriguingly, localization of TbCentrin4 was dispersed or disappeared from basal bodies and the bi-lobe structure when the cells were treated with Ca2+ in vivo, implying the influence of Ca2+ on the cellular functions of TbCentrin4. Besides, we observed the interactions between TbCentrin4 and other Tbcentrins and revealed that the interactions are Ca2+ dependent. Our findings provide a structural basis for better understanding the biological functions of TbCentrin4 in the relevant cellular processes.
WOS关键词EF-HAND ; PROTEIN ; BINDING ; YEAST ; CALMODULIN ; CALCIUM ; CELL ; CENTROSOMES ; APOPTOSIS ; AUTOPHAGY
资助项目National Natural Science Foundation of China[31270780] ; National Natural Science Foundation of China[U1332137] ; National Natural Science Foundation of China[31500601] ; National Natural Science Foundation of China[31570737]
WOS研究方向Biochemistry & Molecular Biology
语种英语
出版者PORTLAND PRESS LTD
WOS记录号WOS:000452401300004
资助机构National Natural Science Foundation of China ; National Natural Science Foundation of China ; National Natural Science Foundation of China ; National Natural Science Foundation of China ; National Natural Science Foundation of China ; National Natural Science Foundation of China ; National Natural Science Foundation of China ; National Natural Science Foundation of China ; National Natural Science Foundation of China ; National Natural Science Foundation of China ; National Natural Science Foundation of China ; National Natural Science Foundation of China ; National Natural Science Foundation of China ; National Natural Science Foundation of China ; National Natural Science Foundation of China ; National Natural Science Foundation of China
源URL[http://ir.hfcas.ac.cn:8080/handle/334002/41078]  
专题医学物理与技术中心
通讯作者Tu, Xiaoming
作者单位1.Univ Sci & Technol China, Hefei Natl Lab Phys Sci Microscale, Hefei, Anhui, Peoples R China
2.Univ Sci & Technol China, Sch Life Sci, Hefei, Anhui, Peoples R China
3.Chinese Acad Sci, Ctr Med Phys & Technol, Anhui Prov Key Lab Med Phys & Technol, Hefei, Anhui, Peoples R China
4.Chinese Acad Sci, Canc Hosp, Hefei, Anhui, Peoples R China
5.Anhui Univ, Sch Life Sci, Hefei, Anhui, Peoples R China
推荐引用方式
GB/T 7714		 Shan, Fangzhen,Ye, Kaiqin,Zhang, Jiahai,et al. Solution structure of TbCentrin4 from Trypanosoma brucei and its interactions with Ca2+ and other centrins[J]. BIOCHEMICAL JOURNAL,2018,475:3763-3778.
APA Shan, Fangzhen.,Ye, Kaiqin.,Zhang, Jiahai.,Liao, Shanhui.,Zhang, Xuecheng.,...&Tu, Xiaoming.(2018).Solution structure of TbCentrin4 from Trypanosoma brucei and its interactions with Ca2+ and other centrins.BIOCHEMICAL JOURNAL,475,3763-3778.
MLA Shan, Fangzhen,et al."Solution structure of TbCentrin4 from Trypanosoma brucei and its interactions with Ca2+ and other centrins".BIOCHEMICAL JOURNAL 475(2018):3763-3778.

入库方式： OAI收割

来源：合肥物质科学研究院

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