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Stabilization of sea urchin flagellar microtubules by histone H1 Luc Multigner*, Jean Gagnon†, Alain Van Dorsselaer‡ & Didier Job*
*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
†Institut de Biologie Structural, 41 avenue des Martyrs, 38027 Grenoble Cedex 1, France
‡Laboratoire de Spectrométrie de Masse Bio-Organique, Faculté de Chimie, 1 rue Blaise Pascal, 67008 Strasbourg Cedex, France
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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