Glycolytic enzyme-tubulin interactions: role of tubulin carboxy terminals

• Published in: Journal of molecular recognition Vol. 6; no. 4; p. 167
• Main Authors: Volker, K W, Knull, H R
• Format: Journal Article
• Language: English
• Published: England 01-12-1993
• Subjects: Amino Acid Sequence; Animals; Cattle; Chromatography, Affinity; Fructose-Bisphosphate Aldolase - antagonists & inhibitors; Glyceraldehyde-3-Phosphate Dehydrogenases - antagonists & inhibitors; Glycolysis - physiology; In Vitro Techniques; Microtubules - chemistry; Microtubules - metabolism; Molecular Sequence Data; Molecular Structure; Peptide Fragments - antagonists & inhibitors; Protein Binding; Protein Conformation; Subtilisins; Tubulin - chemistry; Tubulin - genetics; Tubulin - metabolism
• ISSN: 0952-3499
• DOI: 10.1002/jmr.300060405

Tubulin and microtubules were modified with the protease, subtilisin. The modification reduced the length of alpha- or beta-tubulin by cleaving a peptide fragment from the C-terminals. Generation of alpha'beta'-tubulin, which is cleaved at both the alpha- and beta-subunit terminals, and alpha beta'-tubulin, which is cleaved at the beta-subunit C-terminal, have already been reported. In this work an isotype, alpha'beta-tubulin, was produced. The three modified tubulin isotypes were compared for their ability to interact with glycolytic enzymes. Cleavage of alpha led to a poorer interaction when tested via affinity chromatography. Tubulin also inhibits the activity of aldolase and glyceraldehyde 3-phosphate dehydrogenase. When the alpha-subunit C-terminal was intact, inhibition was greatest. These results imply that the C-terminal of the tubulin alpha-subunit is responsible for interactions with glycolytic enzymes.