Predation by the sea otter (Enhydra lutris) limits epibenthic invertebrates, especially sea urchins (Strongylocentrotus polyacanthus), in turn allowing a luxuriant development of the macroalgal canopy. Where sea otters are abundant, sea urchins are small and scarce in shallow water, and the association of fleshy macroalgae apparently is regulated by competition. Sea urchins are larger and more abundant in deeper water, where they are less accessible to sea otters. Macroalgae are most abundant, and competition in the plant association is severest, near the sublittoral fringe where sea otters can remove sea urchins most efficiently. In deep water, competition among maccroalgae is reduced because the light intensity is lower and grazing by sea urchins increases. On islands where sea otters are absent, sea urchins are abundant, large, and are probably limited by intraspecific competition; and they have eliminated fleshly macroalgae. Available data suggest that the association of Laminaria spp. and Agarum cribrosum contributes most to primary production in nearshore areas of the western Aleutian Islands. Where sea otters are absent and sea urchins have eliminated this plant association, some higher trophic forms also are absent or less abundant than where sea otters are common and the plant association is well developed. Earlier studies of sea otter food suggested that low—density populations of sea otters consume primarily sea urchins and mollusks in the western Aleutian Islands. Later studies of high—density populations showed a wider variety of foods consumed, with fish an important component of the diet. These studies support our observations on the differences in availability of these foods between islands with and without sea otters.
Actin is known to undergo reversible monomer-polymer transitions that coincide with various cell activities such as cell shape changes, locomotion, endocytosis and exocytosis. This dynamic state of actin filament self-assembly and disassembly is thought to be regulated by the properties of the monomeric actin molecule and in vivo by the influence of actin-associated proteins. Of major importance to the properties of the monomeric actin molecule are the presence of one tightly-bound ATP and one tightly-bound divalent cation per molecule. In vivo the divalent cation is thought to be Mg2+ (Mg-actin) but in vitro standard purification procedures result in the preparation of Ca-actin. The affinity of actin for a divalent cation at the tight binding site is in the nanomolar range, much higher than earlier thought. The binding kinetics of Mg2+ and Ca2+ at the high affinity site on actin are considered in terms of a simple competitive binding mechanism. This model adequately describes the published observations regarding divalent cation exchange on actin. The effects of the tightly-bound cation, Mg2+ or Ca2+, on nucleotide binding and exchange on actin, actin ATP hydrolysis activity and nucleation and polymerization of actin are discussed. From the characteristics that are reviewed, it is apparent that the nature of the bound divalent cation has a significant effect on the properties of actin.
Under conditions where muscle actin only partially polymerizes, or where it does not polymerize at all, a significant enhancement of polymerization was observed if equimolar phalloidin was also present. The increased extent of polymerization in the the presence of phalloidin can be explained by the reduced critical actin concentration of partially polymerized populations at equilibrium. Under such conditions, the rate of polymerization, as judged by the length of time to reach half the viscosity plateau, was found to be essentially independent of the phalloidin concentration. Moreover, the initial rate of polymerization of actin was also found to be independent of phalloidin concentration. However, phalloidin apparently causes a reduction in the magnitude of the reverse rates in the polymerization reaction, as was demonstrated by the lack of depolymerization of phalloidin-treated actin polymers. This effect of phalloidin is also supported by the identification of actin nuclei and short polymers in populations of G-actin incubated with phalloidin in the absence of added KCl. Our conclusion, then, is that phalloidin influences the polymerization of actin by stabilizing nuclei and polymers as they are formed.
We have quantitated the in vitro interactions of profilin and the profilin-actin complex (PA) with the actin filament barbed end using profilin and nonmuscle beta,gamma-actin prepared from bovine spleen. Actin filament barbed end elongation was initiated from spectrin seeds in the presence of varying profilin concentrations and followed by light scattering. We find that profilin inhibits actin polymerization and that this effect is much more pronounced for beta,gamma-actin than for alpha-skeletal muscle actin. Profilin binds to beta,gamma-actin filament barbed ends with an equilibrium constant of 20 microM, decreases the filament elongation rate by blocking addition of actin monomers, and increases the dissociation rate of actin monomers from the filament end. PA containing bound MgADP supports elongation of the actin filament barbed end, indicating that ATP hydrolysis is not necessary for PA elongation of filaments. Initial analysis of the energetics for these reactions suggested an apparent greater negative free energy change for actin filament elongation from PA than elongation from monomeric actin. However, we calculate that the free energy changes for the two elongation pathways are equal if the profilin-induced weakening of nucleotide binding to actin is taken into consideration.
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