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. 1993 Feb 1;289(Pt 3):897–902. doi: 10.1042/bj2890897

Proteolytic removal of three C-terminal residues of actin alters the monomer-monomer interactions.

M Mossakowska 1, J Moraczewska 1, S Khaitlina 1, H Strzelecka-Golaszewska 1
PMCID: PMC1132260  PMID: 8435084

Abstract

Homogeneous preparations of actin devoid of the three C-terminal residues were obtained by digestion of G-actin with trypsin after blocking proteolysis at other sites by substitution of Mg2+ for the tightly bound Ca2+. Removal of the C-terminal residues resulted in the following: an enhancement of the Mg(2+)-induced hydrolysis of ATP in low-ionic-strength solutions of actin; an increase in the critical concentration for polymerization; a decrease in the initial rate of polymerization; and an enhancement of the steady-state exchange of subunits in the polymer. Electron microscopy indicated an increased fragility of the filaments assembled from truncated actin. The results suggest that removal of the C-terminal residues increases the rate constants for monomer dissociation from the polymer ends and from the oligomeric species.

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Selected References

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