title: Tubulin assembly is disordered in a hypogeomagnetic field.
abstract: Although the effect of a magnetic field on functions of many proteins has been reported, tubulin assembly in a hypogeomagnetic field (HGMF) has not yet been characterized. Here, we show disorder in tubulin self-assembly in an HGMF. Absorbance at 350 nm, commonly used to monitor tubulin self-assembly, was altered in the HGMF, providing evidence for the effects of HGMF on tubulin. Measurements of intrinsic fluorescence (335 nm) also revealed a disordered change in tubulin conformation during assembly in the HGMF. Under the same conditions, microtubule-like filaments were not observed by electron microscopy, with the exception of amorphous oligomers. Incubation of tubulin with tau in the natural geomagnetic field (GMF) yielded microtubule-like filaments, while only amorphous oligomers were observed following the incubation in the HGMF. This distinction suggests that tubulin assembly depends upon the GMF, and that elimination of the GMF induces disorder in tubulin organization.
authors.affiliation: State Key Laboratory of Brain and Cognitive Sciences, Institute of Biophysics, Chinese Academy of Sciences, 15 Da Tun Road, Chaoyang District, Beijing 100101, China.
authors.forename: Dong Liang
authors.initials: DL
authors.lastname: Wang
authors.forename: Xing Sheng
authors.initials: XS
authors.lastname: Wang
authors.forename: Rong
authors.initials: R
authors.lastname: Xiao
authors.forename: Ying
authors.initials: Y
authors.lastname: Liu
authors.forename: Rong Qiao
authors.initials: RQ
authors.lastname: He
mesh_terms: D006801:Humans; D008280:Magnetics; D014404:Tubulin / Q000737:chemistry* / Q000648:ultrastructure*; D016875:tau Proteins / Q000737:chemistry
chemical_list: D014404:Tubulin; D016875:tau Proteins