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The solution structure of the N-terminal domain of human tubulin binding cofactor C reveals a platform for tubulin interaction

Abstract: Human Tubulin Binding Cofactor C (TBCC) is a post-chaperonin involved in the folding and assembly of ?- and ?-tubulin monomers leading to the release of productive tubulin heterodimers ready to polymerize into microtubules. In this process it collaborates with other cofactors (TBC's A, B, D, and E) and forms a supercomplex with TBCD, ?-tubulin, TBCE and ?-tubulin. Here, we demonstrate that TBCC depletion results in multipolar spindles and mitotic failure. Accordingly, TBCC is found at the centrosome and is implicated in bipolar spindle formation. We also determine by NMR the structure of the N-terminal domain of TBCC. The TBCC N-terminal domain adopts a spectrin-like fold topology composed of a left-handed 3-stranded ?-helix bundle. Remarkably, the 30-residue N-terminal segment of the TBCC N-terminal domain is flexible and disordered in solution. This unstructured region is involved in the interaction with tubulin. Our data lead us to propose a testable model for TBCC N-terminal domain/tubulin recognition in which the highly charged N-terminus as well as residues from the three helices and the loops interact with the acidic hypervariable regions of tubulin monomers.

Otras publicaciones de la misma revista o congreso con autores/as de la Universidad de Cantabria

 Autoría: Garcia-Mayoral M., Castaño R., Fanarraga M., Zabala J., Rico M., Bruix M.,

 Fuente: PLoS ONE, 2011, 6(10), e25912

Editorial: Public Library of Science

 Fecha de publicación: 01/10/2011

Nº de páginas: 12

Tipo de publicación: Artículo de Revista

 DOI: 10.1371/journal.pone.0025912

ISSN: 1932-6203

 Proyecto español: CSD2006-00023

Url de la publicación: https://doi.org/10.1371/journal.pone.0025912