Conformational changes in actin induced by its interaction with gelsolin

Khaitlina S, Hinssen H (1997)
BIOPHYSICAL JOURNAL 73(2): 929-937.

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Actin cleaved by the protease from Escherichia coli A2 strain between Gly(42) and Val(43) (ECP-actin) is no longer polymerizable when it contains Ca2+ as a tightly bound cation, but polymerizes when Mg2+ is bound. We have investigated the interactions of gelsolin with this actin with regard to conformational changes in the actin molecule induced by the binding of gelsolin, ECP-(Ca)actin interacts with gelsolin in a manner similar to that in which it reacts with intact actin, and forms a stoichiometric 2:1 complex. Despite the nonpolymerizabilty of ECP-(Ca)actin, this complex can act as a nucleus for the polymerization of intact actin, thus indicating that upon interaction with gelsolin, ECP-(Ca)actin undergoes a conformational change that enables its interaction with another actin monomer, By gel filtration and fluorometry it was shown that the binding of at least one of the ECP-cleaved actins to gelsolin is considerably weaker than of intact actin, suggesting that conformational changes in subdomain 2 of actin monomer may directly or allosterically affect actin-gelsolin interactions. On the other hand, interaction with gelsolin changes the conformation of actin within the DNase I-binding loop, as indicated by inhibition of limited proteolysis of actin by ECP and subtilisin. Cross-linking experiments with gelsolin-nucleated actin filaments using N,N-phenylene-bismaleimide (which cross-links adjacent actin monomers between Cys(374) and Lys(191)) reveal that gelsolin causes a significant increase in the yield of the 115-kDa cross-linking product, confirming the evidence that gelsolin stabilizes or changes the conformation of the C-terminal region of the actin molecule, and these changes are propagated from the capped end along the filament. These results allow us to conclude that nucleation of actin polymerization by gelsolin is promoted by conformational changes within subdomain 2 and at the C-terminus of the actin monomer.
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Khaitlina S, Hinssen H. Conformational changes in actin induced by its interaction with gelsolin. BIOPHYSICAL JOURNAL. 1997;73(2):929-937.
Khaitlina, S., & Hinssen, H. (1997). Conformational changes in actin induced by its interaction with gelsolin. BIOPHYSICAL JOURNAL, 73(2), 929-937.
Khaitlina, S., and Hinssen, H. (1997). Conformational changes in actin induced by its interaction with gelsolin. BIOPHYSICAL JOURNAL 73, 929-937.
Khaitlina, S., & Hinssen, H., 1997. Conformational changes in actin induced by its interaction with gelsolin. BIOPHYSICAL JOURNAL, 73(2), p 929-937.
S. Khaitlina and H. Hinssen, “Conformational changes in actin induced by its interaction with gelsolin”, BIOPHYSICAL JOURNAL, vol. 73, 1997, pp. 929-937.
Khaitlina, S., Hinssen, H.: Conformational changes in actin induced by its interaction with gelsolin. BIOPHYSICAL JOURNAL. 73, 929-937 (1997).
Khaitlina, S, and Hinssen, Horst. “Conformational changes in actin induced by its interaction with gelsolin”. BIOPHYSICAL JOURNAL 73.2 (1997): 929-937.
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Functions of gelsolin: motility, signaling, apoptosis, cancer.
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Epigenetic regulation of gelsolin expression in human breast cancer cells.
Mielnicki LM, Ying AM, Head KL, Asch HL, Asch BB., Exp. Cell Res. 249(1), 1999
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Defining actin filament length in striated muscle: rulers and caps or dynamic stability?
Littlefield R, Fowler VM., Annu. Rev. Cell Dev. Biol. 14(), 1998
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30 References

Data provided by Europe PubMed Central.

Long-range conformational effects of proteolytic removal of the last three residues of actin.
Strzelecka-Golaszewska H, Mossakowska M, Wozniak A, Moraczewska J, Nakayama H., Biochem. J. 307 ( Pt 2)(), 1995
PMID: 7733893
[Protease from a strain of bacteria E. coli A2, specifically cleaving actin]
Usmanova AM, Khaitlina SIu., Biokhimiia 54(8), 1989
PMID: 2684280
Interactions of pig plasma gelsolin with G-actin.
Weeds AG, Harris H, Gratzer W, Gooch J., Eur. J. Biochem. 161(1), 1986
PMID: 3023088

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