An Atomistic View of Microtubule Stabilization by GTP - Archive ouverte HAL
Article Dans Une Revue Structure Année : 2013

An Atomistic View of Microtubule Stabilization by GTP

Résumé

A microtubule is a dynamic system formed of ab-tubulins. The presence of nonhydrolyzable guanosine-50-triphosphate (GTP)/guanosine diphosphate (GDP) on the b-tubulins provokes microtubule polymerization/depolymerization. Despite the large number of experimental studies of this dynamical process, its mechanism is still unclear. To provide insights into this mechanismwe studied the first depolymerization steps of GDP/GTP-bound microtubules by normal-mode analysis with the all-atom model. We also constructed a depolymerizing microtubule and compared it to cryo-electron microscopy tomograms (cyro-ET). The results show that during depolymerization, the protofilaments not only curve but twist to weaken their lateral interactions. These interactions are stabilized by GTP, but not evenly. Not all of the interface residues are of equal importance: five of them, belonging to the H2-S3 loop, play a special role; acting as a lock whose key is the g-phosphate of GTP. Sequence alignments of several tubulins confirm the importance of these residues.

Dates et versions

hal-04489203 , version 1 (04-03-2024)

Identifiants

Citer

Eric Quiniou, Paul Guichard, David Perahia, Sergio Marco, Liliane Mouawad. An Atomistic View of Microtubule Stabilization by GTP. Structure, 2013, 21 (5), pp.833-843. ⟨10.1016/j.str.2013.03.009⟩. ⟨hal-04489203⟩
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