65 research outputs found
Polyamine Sharing between Tubulin Dimers Favours Microtubule Nucleation and Elongation via Facilitated Diffusion
We suggest for the first time that the action of multivalent cations on
microtubule dynamics can result from facilitated diffusion of GTP-tubulin to the
microtubule ends. Facilitated diffusion can promote microtubule assembly,
because, upon encountering a growing nucleus or the microtubule wall, random
GTP-tubulin sliding on their surfaces will increase the probability of
association to the target sites (nucleation sites or MT ends).
This is an original explanation for understanding the apparent discrepancy
between the high rate of microtubule elongation and the low rate of tubulin
association at the microtubule ends in the viscous cytoplasm. The mechanism of
facilitated diffusion requires an attraction force between two tubulins, which
can result from the sharing of multivalent counterions. Natural polyamines
(putrescine, spermidine, and spermine) are present in all
living cells and are potent agents to trigger tubulin self-attraction. By using
an analytical model, we analyze the implication of facilitated diffusion
mediated by polyamines on nucleation and elongation of microtubules. In
vitro experiments using pure tubulin indicate that the promotion of
microtubule assembly by polyamines is typical of facilitated diffusion. The
results presented here show that polyamines can be of particular importance for
the regulation of the microtubule network in vivo and provide
the basis for further investigations into the effects of facilitated diffusion
on cytoskeleton dynamics
Strength gain through eccentric isotonic training without changes in clinical signs or blood markers
Subnanometer atomic force microscopy of peptide–mineral interactions links clustering and competition to acceleration and catastrophe
In vitro observations have revealed major effects on the structure, growth, and composition of biomineral phases, including stabilization of amorphous precursors, acceleration and inhibition of kinetics, and alteration of impurity signatures. However, deciphering the mechanistic sources of these effects has been problematic due to a lack of tools to resolve molecular structures on mineral surfaces during growth. Here we report atomic force microscopy investigations using a system designed to maximize resolution while minimizing contact force. By imaging the growth of calcium-oxalate monohydrate under the influence of aspartic-rich peptides at single-molecule resolution, we reveal how the unique interactions of polypeptides with mineral surfaces lead to acceleration, inhibition, and switching of growth between two distinct states. Interaction with the positively charged face of calcium-oxalate monohydrate leads to formation of a peptide film, but the slow adsorption kinetics and gradual relaxation to a well-bound state result in time-dependent effects. These include a positive feedback between peptide adsorption and step inhibition described by a mathematical catastrophe that results in growth hysteresis, characterized by rapid switching from fast to near-zero growth rates for very small reductions in supersaturation. Interactions with the negatively charged face result in formation of peptide clusters that impede step advancement. The result is a competition between accelerated solute attachment and inhibition due to blocking of the steps by the clusters. The findings have implications for control of pathological mineralization and suggest artificial strategies for directing crystallization
Sensitivity of floodplain geoecology to human impact: A Holocene perspective for the headwaters of the Dijle catchment, central Belgium
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