DNase I increases the rate constant of depolymerization at the pointed (-) end of actin filaments.
We show here that DNase is distinguished from other known actin-binding proteins by its unique ability to increase the depolymerization rate constant of actin at the pointed filament end, thereby speeding up depolymerization of filaments capped at their barbed ends. This action requires relatively high DNase concentrations, 3 orders of magnitude higher than those needed to block elongation, although 10 times lower than those needed for DNase binding to the side of the filament. We propose that a high DNase concentrations, steric interference between the two DNase molecules, bound to the ends of both strands of the two-start actin helix, destabilizes actin binding to the filament.
Weber
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A
Department of Biochemistry, University of Pennsylvania, Philadelphia 19104.
Pennise
C R
CR
Pring
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M
D000199:Actins / Q000378:metabolism*; D001704:Biopolymers / Q000378:metabolism; D003850:Deoxyribonuclease I / Q000378:metabolism*; D018260:Gelsolin / Q000378:metabolism; D007700:Kinetics; D008956:Models, Chemical; D011485:Protein Binding; D013050:Spectrometry, Fluorescence
D000199:Actins; D001704:Biopolymers; D018260:Gelsolin; D003850:Deoxyribonuclease I