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Stabilization of sea urchin flagellar microtubules by histone H1

Nature volume 360, pages 33–39 (1992)Cite this article

Abstract

Complex microtubule assemblies are essential components of eukaryotic cilia and flagella. They are extremely stable and are not affected by agents that normally induce polymer disassembly. The molecular basis of this microtubular stability is unknown, and it is not related to any feature of the constitutive tubulin. In sea urchin sperm flagella, axonemal microtubules are found to be stabilized by a protein identical to histone H1, a result that defines a new role for this histone and provides evidence for a concerted evolution of chromatin and microtubular structures.

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Authors and Affiliations

  1. Département de Biologie Moléculaire et Structural, Laboratoire du Cytosquelette, Unité INSERM 244, Centre d'Etudes Nucléates de Grenoble, BP 85 X, 38041, Grenoble Cedex, France

    Luc Multigner & Didier Job

  2. Institut de Biologie Structural, 41 avenue des Martyrs, 38027, Grenoble, Cedex 1, France

    Jean Gagnon

  3. Laboratoire de Spectrométrie de Masse Bio-Organique, Faculté de Chimie, 1 rue Blaise Pascal, 67008, Strasbourg Cedex, France

    Alain Van Dorsselaer

Authors
  1. Luc Multigner
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  2. Jean Gagnon
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  3. Alain Van Dorsselaer
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  4. Didier Job
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Multigner, L., Gagnon, J., Van Dorsselaer, A. et al. Stabilization of sea urchin flagellar microtubules by histone H1. Nature 360, 33–39 (1992). https://doi.org/10.1038/360033a0

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