Glycolytic enzyme-tubulin interactions: role of tubulin carboxy terminals.
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.
Volker
K W
KW
Department of Biochemistry and Molecular Biology, School of Medicine, University of North Dakota, Grand Forks 58202.
Knull
H R
HR
D000595:Amino Acid Sequence; D000818:Animals; D002417:Cattle; D002846:Chromatography, Affinity; D005634:Fructose-Bisphosphate Aldolase / Q000037:antagonists & inhibitors; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases / Q000037:antagonists & inhibitors; D006019:Glycolysis / Q000502:physiology*; D066298:In Vitro Techniques; D008870:Microtubules / Q000737:chemistry / Q000378:metabolism; D008969:Molecular Sequence Data; D015394:Molecular Structure; D010446:Peptide Fragments / Q000037:antagonists & inhibitors; D011485:Protein Binding; D011487:Protein Conformation; D013381:Subtilisins; D014404:Tubulin / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*
D010446:Peptide Fragments; D014404:Tubulin; C068142:glyceraldehyde 3-phosphate dehydrogenase (304-313); D005987:Glyceraldehyde-3-Phosphate Dehydrogenases; D013381:Subtilisins; D005634:Fructose-Bisphosphate Aldolase