Open AccessPrecursors of the nerve growth factor γ subunit and renin bind to microtubules
Author(s) -
DICOU Eleni,
BRACHET Philippe
Publication year - 1984
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1984.tb08384.x
Subject(s) - microtubule , tubulin , protein subunit , reticulocyte , affinity chromatography , sepharose , biology , translation (biology) , biochemistry , immunoprecipitation , microtubule associated protein , microbiology and biotechnology , chemistry , rna , messenger rna , enzyme , gene
Translation products of a reticulocyte lysate reaction, programmed with poly(A)‐rich RNAs from the male mouse submaxillary gland, were subjected to affinity chromatography on a tubulin‐Sepharose column. Analysis of the bound proteins in sodium dodecylsulfate/polyacrylamide gels revealed two polypeptides of M r 27000 and 45 000, that were shown to bind to tubulin in a specific manner. These polypeptides were absent from the translation products coded by poly(A)‐rich RNAs from the female mouse. They were eluted from the tubulin‐Sepharose resin under conditions similar to those employed for the dissociation of immune complexes. The M r ‐27000 and M r ‐45000 proteins were identified by immunoprecipitation with specific antisera as the precursors of the γ subunit of the nerve growth factor (NGF) and renin respectively. These two precursors as well as a third, unidentified polypeptide of M r 38000, probably unrelated to the β subunit of NGF, bound also to microtubules. The mature form of renin, purified from the submaximillary gland, also displayed an affinity for the microtubules. In contrast, the mature form of the γ subunit of NGF did not bind to the microtubules. The possible involvement of the microtubules (tubulin) in the biosynthesis of these two secretory proteins is discussed.