Tubulin, but not microtubules, is the substrate for tubulin:tyrosine ligase in mature avian erythrocytes

Chicken erythrocytes, which contain a marginal band of microtubules, were used to study the influence of the aggregation state of tubulin on the post-translational incorporation of tyrosine into the alpha-tubulin subunit. We found that the incorporation of [14C]tyrosine occurs almost exclusively int...

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Bibliographic Details
Published in:The Journal of biological chemistry 1987-11, Vol.262 (32), p.15673-15677
Main Authors: Beltramo, D M, Arce, C A, Barra, H S
Format: Article
Language:English
Subjects:
Animals
Biological and medical sciences
Carboxypeptidases - metabolism
Carboxypeptidases A
Cell structures and functions
CHICKENS
CULTURE MEDIA
Cytoskeleton, cytoplasm. Intracellular movements
Electrophoresis, Polyacrylamide Gel
ERITROCITOS
ERYTHROCYTE
ERYTHROCYTES
Erythrocytes - enzymology
Fundamental and applied biological sciences. Psychology
LIGASA
LIGASE
LIGASES
MADUREZ
MATURITE
MATURITY
MEDIO DE CULTIVO
Microscopy, Electron
Microtubules - metabolism
MILIEU DE CULTURE
Molecular and cellular biology
Peptide Synthases - blood
POLLO
POULET
TIROSINA
tubulin
Tubulin - blood
tubulin:tyrosine ligase
TYROSINE
Tyrosine - metabolism
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Summary:Chicken erythrocytes, which contain a marginal band of microtubules, were used to study the influence of the aggregation state of tubulin on the post-translational incorporation of tyrosine into the alpha-tubulin subunit. We found that the incorporation of [14C]tyrosine occurs almost exclusively into the nonassembled tubulin pool. The marginal band was practically not labeled. The low incorporation into microtubules was not due to the lack of tubulin with acceptor capacity since after cold-induced disassembly, an additional amount of [14C]tyrosine could be incorporated. 14C-Tyrosinated tubulin of the nonassembled pool could not be incorporated into microtubules of the marginal band after prolonged incubation at 37 degrees C or when the marginal band was regenerated after cold-induced depolymerization. In erythrocytes, tubulin:tyrosine ligase behaved as a soluble entity when the cells were lysed under microtubule-preserving conditions.
ISSN:0021-9258
1083-351X
DOI:10.1016/S0021-9258(18)47779-4