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Gelsolin Has Three Actin-binding Sites by J Bryan is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.
What is Gelsolin Has Three Actin-binding Sites about?
Gelsolin, a Ca2+-modulated actin filament-capping and -severing protein, complexes with two actin monomers. Studies designed to localize binding sites on proteolytic fragments identify three distinct actin-binding peptides. 14NT, a 14-kD fragment that contains the NH2 terminal, will depolymerize F-actin. This peptide forms a 1:1 complex with G-actin which blocks the exchange of etheno-ATP from bound actin. The estimated association and dissociation rates for this complex are 0.3 microM-1 s-1 and 1.35 x 10(-6) s-1 which gives a maximum calculated Kd = 4.5 x 10(-12) M. 26NT, the adjacent peptide on the NH2-terminal half of gelsolin, binds to both G- and F-actin. This fragment has little or no intrinsic severing activity and will bind to F-actin to nearly stoichiometric ratios. The interactions of 14NT and 26NT with actin are largely Ca2+ independent and one of these sites, probably 14NT, is the EGTA-stable site identified in the intact protein. 41CT, the COOH-terminal half of gelsolin, forms a rapidly reversible 1:1 complex with actin, Kd = 25 nM, that slows but does not block etheno- ATP exchange. This interaction is Ca2+ dependent and is the exchangeable site in the intact protein.
Who reads Gelsolin Has Three Actin-binding Sites?
It is typically read by researchers, students, and practitioners in Biochemistry, Genetics and Molecular Biology.
- Author
- J Bryan
- Publisher
- The Rockefeller University Press
- Published
- 1988
- Language
- EN
- Field
- Biochemistry, Genetics and Molecular Biology (Life Sciences)