The Ca(2+)-induced conformational change of gelsolin is located in the carboxyl-terminal half of the molecule

Hellweg T, Hinssen H, Eimer W (1993)
Biophysical Journal 65(2): 799-805.

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Zeitschriftenaufsatz | Veröffentlicht | Englisch
Abstract / Bemerkung
We have purified the two functionally distinct domains of gelsolin, a Ca(2+)-dependent actin binding protein, by proteolytic cleavage and characterized their size and shape in solution by dynamic light scattering. In the absence of calcium we obtained the same translational diffusion coefficient for both fragments which are of approximately equal molecular mass. The frictional ratio fo/fexp (1.33-1.39) is similar to the value as obtained for intact gelsolin (1.37) in aqueous solution (Patkowski, A., J. Seils, H. Hinssen, and T. Dorfmüller. 1990. Biopolymers. 30:427-435), indicating a similar molecular shape for the native protein as well as for the two subdomains. Upon addition of Ca2+ the translational diffusion coefficient of the carboxyl-terminal half decreased by almost 10%, while there was no change observed for the amino terminus. This result indicates that the ligand-induced conformational change as seen for intact gelsolin is probably located on the carboxyl-terminal domain of the protein. Since gelsolin has binding sites in both domains, and the isolated amino terminus binds and severs actin in a calcium-independent manner, our results suggests that the structural transition in the carboxyl-terminal part of intact gelsolin also affects the actin binding properties of the amino-terminal half.
Erscheinungsjahr
Zeitschriftentitel
Biophysical Journal
Band
65
Zeitschriftennummer
2
Seite
799-805
ISSN
PUB-ID

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Hellweg T, Hinssen H, Eimer W. The Ca(2+)-induced conformational change of gelsolin is located in the carboxyl-terminal half of the molecule. Biophysical Journal. 1993;65(2):799-805.
Hellweg, T., Hinssen, H., & Eimer, W. (1993). The Ca(2+)-induced conformational change of gelsolin is located in the carboxyl-terminal half of the molecule. Biophysical Journal, 65(2), 799-805. doi:10.1016/S0006-3495(93)81121-4
Hellweg, T., Hinssen, H., and Eimer, W. (1993). The Ca(2+)-induced conformational change of gelsolin is located in the carboxyl-terminal half of the molecule. Biophysical Journal 65, 799-805.
Hellweg, T., Hinssen, H., & Eimer, W., 1993. The Ca(2+)-induced conformational change of gelsolin is located in the carboxyl-terminal half of the molecule. Biophysical Journal, 65(2), p 799-805.
T. Hellweg, H. Hinssen, and W. Eimer, “The Ca(2+)-induced conformational change of gelsolin is located in the carboxyl-terminal half of the molecule”, Biophysical Journal, vol. 65, 1993, pp. 799-805.
Hellweg, T., Hinssen, H., Eimer, W.: The Ca(2+)-induced conformational change of gelsolin is located in the carboxyl-terminal half of the molecule. Biophysical Journal. 65, 799-805 (1993).
Hellweg, Thomas, Hinssen, Horst, and Eimer, W. “The Ca(2+)-induced conformational change of gelsolin is located in the carboxyl-terminal half of the molecule”. Biophysical Journal 65.2 (1993): 799-805.

30 Zitationen in Europe PMC

Daten bereitgestellt von Europe PubMed Central.

Actin-titin interaction in cardiac myofibrils: probing a physiological role.
Linke WA, Ivemeyer M, Labeit S, Hinssen H, Rüegg JC, Gautel M., Biophys J 73(2), 1997
PMID: 9251807
The crystal structure of plasma gelsolin: implications for actin severing, capping, and nucleation.
Burtnick LD, Koepf EK, Grimes J, Jones EY, Stuart DI, McLaughlin PJ, Robinson RC., Cell 90(4), 1997
PMID: 9288746
Multiple pathways for denaturation of horse plasma gelsolin.
Koepf EK, Burtnick LD., Biochem Cell Biol 74(1), 1996
PMID: 9035683

26 References

Daten bereitgestellt von Europe PubMed Central.

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