Calcium-induced conformational changes in the C-terminal half of gelsolin stabilize its interaction with the actin monomer

Khaitlina S, Walloscheck M, Hinssen H (2004)
BIOCHEMISTRY 43(40): 12838-12845.

Zeitschriftenaufsatz | Veröffentlicht | Englisch
 
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Abstract / Bemerkung
The basic mechanism for the nucleating effect of gelsolin on actin polymerization is the formation of a complex of gelsolin with two actin monomers. Probably due to changes in the C-terminal part of gelsolin, a stable ternary complex is only formed at [Ca2+] > 10(-5) M [Khaitlina, S., and Hinssen, H. (2002) FEBS Lett. 521, 14-18]. Therefore, we have studied the binding of actin monomer to the isolated C-terminal half of gelsolin (segments 4-6) over a wide range of calcium ion concentrations to correlate the conformational changes to the complex formation. With increasing [Ca2+], the apparent size of the C-terminal half as determined by gel filtration was reduced, indicating a transition into a more compact conformation. Moreover, Ca2+ inhibited the cleavage by trypsin at Lys 634 within the loop connecting segments 5 and 6. Though the inhibitory effect was observed already at [Ca2+] of 10(-7) M, it was enhanced with increasing [Ca2+], attaining saturation only at > 10(-4) M Ca2+. This indicates that the initial conformational changes are followed by additional molecular transitions in the range of 10(-5)-10(-4) M [Ca2+]. Consistently, preformed complexes of actin with the C-terminal part of gelsolin became unstable upon lowering the calcium ion concentrations. These data provide experimental support for the role of the type 2 Ca-binding sites in gelsolin segment 5 proposed by structural studies [Choe et al. (2002) J. Mol. Biol. 324, 691]. We assume that the observed structural transitions contribute to the stable binding of the second actin monomer in the ternary gelsolin-actin complex.
Erscheinungsjahr
2004
Zeitschriftentitel
BIOCHEMISTRY
Band
43
Ausgabe
40
Seite(n)
12838-12845
ISSN
0006-2960
eISSN
1520-4995
Page URI
https://pub.uni-bielefeld.de/record/1606305

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Khaitlina S, Walloscheck M, Hinssen H. Calcium-induced conformational changes in the C-terminal half of gelsolin stabilize its interaction with the actin monomer. BIOCHEMISTRY. 2004;43(40):12838-12845.
Khaitlina, S., Walloscheck, M., & Hinssen, H. (2004). Calcium-induced conformational changes in the C-terminal half of gelsolin stabilize its interaction with the actin monomer. BIOCHEMISTRY, 43(40), 12838-12845. doi:10.1021/bi049548z
Khaitlina, S., Walloscheck, M., and Hinssen, H. (2004). Calcium-induced conformational changes in the C-terminal half of gelsolin stabilize its interaction with the actin monomer. BIOCHEMISTRY 43, 12838-12845.
Khaitlina, S., Walloscheck, M., & Hinssen, H., 2004. Calcium-induced conformational changes in the C-terminal half of gelsolin stabilize its interaction with the actin monomer. BIOCHEMISTRY, 43(40), p 12838-12845.
S. Khaitlina, M. Walloscheck, and H. Hinssen, “Calcium-induced conformational changes in the C-terminal half of gelsolin stabilize its interaction with the actin monomer”, BIOCHEMISTRY, vol. 43, 2004, pp. 12838-12845.
Khaitlina, S., Walloscheck, M., Hinssen, H.: Calcium-induced conformational changes in the C-terminal half of gelsolin stabilize its interaction with the actin monomer. BIOCHEMISTRY. 43, 12838-12845 (2004).
Khaitlina, S, Walloscheck, M, and Hinssen, Horst. “Calcium-induced conformational changes in the C-terminal half of gelsolin stabilize its interaction with the actin monomer”. BIOCHEMISTRY 43.40 (2004): 12838-12845.

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