Microfilament gel rigidity cooperates negatively with the binding of actin gelling proteins.
At 37 degrees C, in the presence of 0.1 M KC1 and 2 mM MgCl2, the binding of alpha-actinin to F-actin increases with the concentration of alpha-actinin but not with the concentration of F-actin. This implies that binding is determined by additional factors, beside the alpha-actinin - F-actin association constant. We propose that one of these factors is the rigidity of the gel, which cooperates negatively to the binding by increasing the work needed to bring two actin filaments at the reaction distance with alpha-actinin.
Grazi
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Istituto di Chimica Biologica, Universita di Ferrara, Italy.
Trombetta
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Guidoboni
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D008841:Actin Cytoskeleton / Q000378:metabolism*; D000185:Actinin / Q000737:chemistry / Q000378:metabolism; D000199:Actins / Q000378:metabolism; D000818:Animals; D005782:Gels; D066298:In Vitro Techniques; D008840:Microfilament Proteins / Q000737:chemistry / Q000378:metabolism*
D000199:Actins; D005782:Gels; D008840:Microfilament Proteins; D000185:Actinin