Zn2+-mediated Structure Formation and Compaction of The “Natively Unfolded” Human Prothymosin α
Document Type
Article
Publication Date
2000
Digital Object Identifier (DOI)
https://doi.org/10.1006/bbrc.1999.2013
Abstract
Human recombinant prothymosin α (ProTα) is known to have coil-like conformation at neutral pH; i.e., it belongs to the class of “natively unfolded” proteins. By means of circular dichroism, SAXS, and ANS fluorescence, we have investigated the effect of several divalent cations on the structure of this protein. Results of these studies are consistent with the conclusion that ProTα conformation is unaffected by large excess of Ca2+, Mg2+, Mn2+, Cu2+, and Ni2+. However, Zn2+ induces compaction and considerable rearrangement of the protein structure. This means that ProTα can specifically interact with Zn2+ (KD ∼ 10−3 M), and such interactions induce folding of the natively unfolded protein into a compact partially folded (premolten globule-like) conformation. It is possible that these structural changes may be important for the function of this protein.
Was this content written or created while at USF?
Yes
Citation / Publisher Attribution
Biochemical and Biophysical Research Communications, v. 267, issue 2, p. 663-668
Scholar Commons Citation
Uversky, Vladimir N.; Gillespie, Joel R.; Millett, Ian S.; Khodyakova, Anna V.; Vasilenko, Raisa N.; Vasiliev, Anatoly M.; Rodionov, Igor L.; Kozlovskaya, Galina D.; Dolgikh, Dmitry A.; Fink, Anthony L.; Doniach, Sebastian; Permyakov, Eugene A.; and Abramov, Vyacheslav M., "Zn2+-mediated Structure Formation and Compaction of The “Natively Unfolded” Human Prothymosin α" (2000). Molecular Medicine Faculty Publications. 659.
https://digitalcommons.usf.edu/mme_facpub/659
