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First published online September 12, 2003
doi: 10.1242/10.1242/jcs.00743

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Characterisation of PGs1, a subunit of a protein complex co-purifying with tubulin polyglutamylase

Catherine Regnard^2,*, Didier Fesquet¹, Carsten Janke¹, Dominique Boucher², Elisabeth Desbruyères², Annette Koulakoff³, Christine Insina¹, Pierre Travo¹ and Bernard Eddé^1,

¹ Centre de Recherches de Biochimie Macromoléculaire, CNRS, 34293 Montpellier, France
² Laboratoire de Biochimie Cellulaire, CNRS, Université Paris 6, 75252 Paris, France
³ INSERM U114, Collège de France, 75005 Paris, France

Author for correspondence (e-mail: edde{at}crbm.cnrs-mop.fr)

Accepted 4 July 2003

Polyglutamylation is a post-translational modification initially discovered on tubulin. It has been implicated in multiple microtubule functions, including neuronal differentiation, axonemal beating and stability of the centrioles, and shown to modulate the interaction between tubulin and microtubule associated proteins. The enzymes catalysing this modification are not yet known. Starting with a partially purified fraction of mouse brain tubulin polyglutamylase, monoclonal antibodies were raised and used to further purify the enzyme by immunoprecipitation. The purified enzyme complex (M_r 360x10³) displayed at least three major polypeptides of 32, 50 and 80x10³, present in stochiometric amounts. We show that the 32x10³ subunit is encoded by the mouse gene GTRGEO22, the mutation of which has recently been implicated in multiple defects in mice, including male sterility. We demonstrate that this subunit, called PGs1, has no catalytic activity on its own, but is implicated in the localisation of the enzyme at major sites of polyglutamylation, i.e. neurones, axonemes and centrioles.

Key words: Axoneme, Cell cycle, Centrosome, Neurone, Polyglutamylation, Tubulin

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