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Wiley, European Journal of Biochemistry, 3(248), p. 840-847, 1997

DOI: 10.1111/j.1432-1033.1997.t01-1-00840.x

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A Putative β‐Tubulin Phosphate‐Binding Motif is Involved in Lateral Microtubule Protofilament Interactions

Journal article published in 1997 by Mar Perez, Kerman Aloria ORCID, Juan Carlos Zabala, Jesus Avila
This paper is available in a repository.
This paper is available in a repository.

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Data provided by SHERPA/RoMEO

Abstract

We have investigated the role of a putative GTP-binding beta-tubulin motif in microtubule polymerization. A peptide containing residues 126-142 of the beta-tubulin subunit (peptide G) was synthesised and an antibody against it raised. Peptide G prevents the binding of GTP to tubulin and also microtubule polymerization but not the formation of vinblastine-induced tubulin spirals, suggesting that it may prevent lateral but not longitudinal tubulin-tubulin interactions. The antibody to peptide G shows little reaction with the interphase microtubule network, mitotic spindles or midbody of cultured cells, whereas it clearly reacts with vinblastine-induced paracrystals. These results suggest that this putative phosphate-binding site present in beta-tubulin could be involved in the lateral tubulin-tubulin interactions along the microtubule structure.