Article
Rapid nucleotide exchange renders Asp-11 mutant actins resistant to depolymerizing activity of cofilin, leading to dominant toxicity in vivo.
The Journal of biological chemistry - 18 Jan 2013
Umeki Nobuhisa, Nakajima Jun, Noguchi Taro Q P, Tokuraku Kiyotaka, Nagasaki Akira, Ito Kohji, Hirose Keiko, Uyeda Taro Q P
Abstract excerpt
Conserved Asp-11 of actin is a part of the nucleotide binding pocket, and its mutation to Gln is dominant lethal in yeast, whereas the mutation to Asn in human α-actin dominantly causes congenital myopathy. To elucidate the molecular mechanism of those dominant negative effects, we prepared Dictyostelium versions of D11N and D11Q mutant actins and characterized them in vitro. D11N and D11Q actins underwent...
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