Abstract
MICROTUBULE assembly in vitro requires (in normal conditions) that GTP be bound to the exchangeable nucleotide-binding site of tubulin1–3. The bound GTP is hydrolysed during polymerisation and the resulting GDP remains bound to the microtubule while the phosphate is released into the medium. Although hydrolysis normally occurs during polymerisation, microtubules will form in a non-hydrolysable analogue of GTP, guanylyl imidodiphosphate (GMP-PNP)4–6. We have observed6, as also has Arai5, that microtubules polymerised in GMP-PNP are not depolymerised by concentrations of Ca which completely depolymerise GTP microtubules. We have now found that GMP-PNP microtubules do not display evidence for a rapid equilibrium between polymer and subunit. The irreversible behaviour of GMP-PNP microtubules may explain the insensitivity to Ca and suggests a function for nucleotide hydrolysis during tubulin polymerisation.
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WEISENBERG, R., DEERY, W. Role of nucleotide hydrolysis in microtubule assembly. Nature 263, 792–793 (1976). https://doi.org/10.1038/263792a0
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DOI: https://doi.org/10.1038/263792a0
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