The Dam1 kinetochore ring complex moves processively on depolymerizing microtubule ends

Article Abstract:

The ten-protein Dam1 complex in budding yeast is a critical microtubule binding component of the kinetochore that oligomerizes into a 50-nm ring around a microtubule in vitro, and it is shown that the ring complex moves processively at the ends of depolymerizing microtubules without detaching from the lattice. The Dam1 ring complex is a molecular device that can translate the force generated by microtubule depolymerization into movement along the lattice to facilitate chromosome segregation.

United States, Microtubules, Ring-opening polymerization

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Structure of tubulin at 6.5 Angstom and location of the taxol-binding site

Article Abstract:

Electron crystallography of zinc-induced two-dimensional crystals of tubulin was performed to enable a three-dimensional reconstruction of tubulin at 6.5-Angstrom resolution. The alpha- and beta- subunits of tubulin appear topologically similar in accordance with their homology of their amino acid sequences. An alpha-helical portion identified at the carboxy terminus of the protein could be the putative binding site for taxol.

Usage, Crystallography, Binding sites (Biochemistry), Active sites (Biochemistry), Tubulins, Tubulin

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Nucleotide-dependent bending flexibility of tubulin regulates microtubule assembly

Article Abstract:

Two structures corresponding to the start and ends in the microtubule polymerization and hydrolysis cycles are presented. It illustrates the consequences of nucleotide state on longitudinal and lateral assembly.

Hydrolysis, DNA microarrays, DNA synthesis

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