Water in actin polymerization.
We have addressed the question whether water is part of the G- to F-actin polymerization reaction. Under osmotic stress, the critical concentration for G-Ca-ATP actin was reduced for six different osmolytes. These results are interpreted as showing that reducing water activity favored the polymerized state. The magnitude of the effect correlated, then saturated, with increasing MW of the osmolyte and suggested that up to 10-12 fewer water molecules were associated with actin when it polymerized. By contrast, osmotic effects were insignificant for Mg-ATP actin. The nucleotide binding site of the Mg conformation is more closed than the Ca and more closely resembles the closed actin conformation in the polymerized state. These results suggest that the water may come from the cleft of the nucleotide binding site.
Fuller
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Department of Biological Sciences, Brock University, St. Catharines, Ontario, Canada.
Rand
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D000199:Actins / Q000737:chemistry*; D000255:Adenosine Triphosphate / Q000737:chemistry; D000818:Animals; D055592:Biophysical Phenomena; D001703:Biophysics; D001704:Biopolymers / Q000737:chemistry; D066298:In Vitro Techniques; D008970:Molecular Weight; D009997:Osmotic Pressure; D011487:Protein Conformation; D011817:Rabbits; D012996:Solutions; D014867:Water / Q000737:chemistry
D000199:Actins; D001704:Biopolymers; D012996:Solutions; D014867:Water; D000255:Adenosine Triphosphate