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

Human Tubulin Binding Cofactor C (TBCC) is a post-chaperonin involved in the folding and assembly of α- and β-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, an...

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Autores principales:	Ma Flor Garcia-Mayoral, Raquel Castaño, Monica L Fanarraga, Juan Carlos Zabala, Manuel Rico, Marta Bruix
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2011
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/3c03cca249f44b35983431540a9b7678
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spelling	oai:doaj.org-article:3c03cca249f44b35983431540a9b76782021-11-18T07:36:19ZThe solution structure of the N-terminal domain of human tubulin binding cofactor C reveals a platform for tubulin interaction.1932-620310.1371/journal.pone.0025912https://doaj.org/article/3c03cca249f44b35983431540a9b76782011-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/22028797/?tool=EBIhttps://doaj.org/toc/1932-6203Human Tubulin Binding Cofactor C (TBCC) is a post-chaperonin involved in the folding and assembly of α- and β-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, β-tubulin, TBCE and α-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 α-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.Ma Flor Garcia-MayoralRaquel CastañoMonica L FanarragaJuan Carlos ZabalaManuel RicoMarta BruixPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 6, Iss 10, p e25912 (2011)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Ma Flor Garcia-Mayoral Raquel Castaño Monica L Fanarraga Juan Carlos Zabala Manuel Rico Marta Bruix The solution structure of the N-terminal domain of human tubulin binding cofactor C reveals a platform for tubulin interaction.
description	Human Tubulin Binding Cofactor C (TBCC) is a post-chaperonin involved in the folding and assembly of α- and β-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, β-tubulin, TBCE and α-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 α-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.
format	article
author	Ma Flor Garcia-Mayoral Raquel Castaño Monica L Fanarraga Juan Carlos Zabala Manuel Rico Marta Bruix
author_facet	Ma Flor Garcia-Mayoral Raquel Castaño Monica L Fanarraga Juan Carlos Zabala Manuel Rico Marta Bruix
author_sort	Ma Flor Garcia-Mayoral
title	The solution structure of the N-terminal domain of human tubulin binding cofactor C reveals a platform for tubulin interaction.
title_short	The solution structure of the N-terminal domain of human tubulin binding cofactor C reveals a platform for tubulin interaction.
title_full	The solution structure of the N-terminal domain of human tubulin binding cofactor C reveals a platform for tubulin interaction.
title_fullStr	The solution structure of the N-terminal domain of human tubulin binding cofactor C reveals a platform for tubulin interaction.
title_full_unstemmed	The solution structure of the N-terminal domain of human tubulin binding cofactor C reveals a platform for tubulin interaction.
title_sort	solution structure of the n-terminal domain of human tubulin binding cofactor c reveals a platform for tubulin interaction.
publisher	Public Library of Science (PLoS)
publishDate	2011
url	https://doaj.org/article/3c03cca249f44b35983431540a9b7678
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The solution structure of the N-terminal domain of human tubulin binding cofactor C reveals a platform for tubulin interaction.

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