Open AccessBundling of microtubules by glyceraldehyde‐3‐phosphate dehydrogenase and its modulation by ATP
Author(s) -
HUITOREL Philippe,
PANTALONI Dominique
Publication year - 1985
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1985.tb09016.x
Subject(s) - tetramer , glyceraldehyde 3 phosphate dehydrogenase , dehydrogenase , tubulin , microtubule , biochemistry , nucleotide , adenosine triphosphate , chemistry , glyceraldehyde , enzyme , biophysics , biology , microbiology and biotechnology , gene
Glyceraldehyde‐3‐phosphate dehydrogenase from different origins (brain, muscle, erythrocytes) binds to microtubules polymerized from pure brain tubulin and causes bundle formation in vitro . ATP is shown to dissociate these bundles into individual microtubules, while the dehydrogenase is not displaced from the polymers by this nucleotide. ATP can be replaced by adenosine 5′‐(ß,γ‐imido]triphosphate, a nonhydrolyzable analog of ATP. These data are interpreted in terms of dissociation of the glyceraldehyde‐3‐phosphate dehydrogenase tetramer into dimers by ATP. The enzyme is also efficiently purified by a tubulin‐Sepharose affinity chromatography.