Fission yeast kinesin-5, cut-7, is the biological motor powered by ATP hydrolysis which plays an essential role in the segregation of chromosomes during the mitotic cell division in eukaryotic cells. The motor protein is a crosslinked homo-tetramer that slides the spindle microtubules towards the spindle poles. However, the mechanisms and functions of cut-7 are largely unknown. In a part, this study focuses on the interaction of the cut7 motor domain with a tubulin heterodimer. Molecular dynamics simulations and various analysis methods were implemented to study the interaction between cut-7 and tubulins. Our primary results suggest the interaction between the motor domain and beta-tubulin is stronger than the motor domain and alpha-tubulin. Moreover, the binding energies, salt bridges, hydrogen bonds, and electrostatic interactions, were analyzed in detail. The key residues at the motor domain and beta, motor domain, and alpha binding interfaces were also identified. This work is useful for discovering inhibitors to develop antiproliferation drugs against cancerous cells and birth-related defects. Since the amino acid sequence of the kinesin motor domain and structures are well conserved among kinesin families, the knowledge acquired in this work can be disseminated to other families of kinesin as well.

Interactions of the kinesin-5 motor domain and tubulins

ACS Fall 2021

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