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Localization and Characterization of Tubulin‐Like Proteins Associated with Brain Mitochondria: The Presence of a Membrane‐Specific Isoform
Author(s) -
Hargreaves Alan J.,
Avila Jesús
Publication year - 1985
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1111/j.1471-4159.1985.tb04015.x
Subject(s) - tubulin , isoelectric point , isoelectric focusing , gene isoform , biology , biochemistry , mitochondrion , microtubule , blot , protein subunit , gel electrophoresis , cell fractionation , microbiology and biotechnology , membrane , enzyme , gene
A mitochondrial fraction, purified from pig brain, was found to contain associated polypeptides with the same electrophoretic migration and isoelectric points as the α‐ and β‐tubulin subunits present in brain microtubules. When analyzed by Western blotting these polypeptides reacted specifically with purified tubulin antibodies. The tubulin‐like proteins were then visualized in mitochondrial membranes by protein A‐gold complexes after the incubation of purified mitochondria with tubulin antibodies. When membrane and microtubule proteins were compared by isoelectric focussing and two‐dimensional gel electrophoresis, differences were observed in the patterns of tubulin isoforms. An additional polypeptide, with the electrophoretic migration of β‐tubulin but the isoelectric point of α‐tubulin, was found to be enriched in the mitochondrial fraction. This peptide had several Staphylococcus aureus V8 protease peptides in common with α‐tubulin and may result from a posttranslational modification of that subunit.