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Gene Review:

TTL - tubulin tyrosine ligase

Bos taurus

Raybin, D. et al., Cutshaw, J.L. et al., Paturle-Lafanechère, L. et al.

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High impact information on LOC514559

Thus, non-tyrosinatable tubulin originates from a well-defined posttranslational modification of the tubulin primary structure which is located at the expected site of activity of tubulin tyrosine ligase [1].
Tubulin--tyrosine ligase is specific for tubulin; other proteins with C-terminal glutamate or glutamine do not substratesmate or glutamine do not act as substrates or inhibitors [2].

Anatomical context of LOC514559

A posttranslational modification of tubulin with potential significance for the regulation of microtubule assembly or function has been revealed by the discovery of an enzyme (tubulin--tyrosine ligase) which can add a tyrosine residue to the alphachain, apparently through peptide bond linkage to a C-terminal glutamate or glutamine [2].

Analytical, diagnostic and therapeutic context of LOC514559

Treatment groups (n = 5 per group) consisted of: 1) control suckled (CS); 2) weaned plus electrical stimulation of the teat (ESTT); 3) weaned plus electrical stimulation of the tail (ESTL); 4) weaned plus thermal stimulation of the teat (TTT); 5) weaned plus thermal stimulation of the tail (TTL) and 6) weaned (WN) [3].

References

Characterization of a major brain tubulin variant which cannot be tyrosinated. Paturle-Lafanechère, L., Eddé, B., Denoulet, P., Van Dorsselaer, A., Mazarguil, H., Le Caer, J.P., Wehland, J., Job, D. Biochemistry (1991) [Pubmed]
Enzyme which specifically adds tyrosine to the alpha chain of tubulin. Raybin, D., Flavin, M. Biochemistry (1977) [Pubmed]
Effects of transcutaneous thermal and electrical stimulation of the teat on pituitary luteinizing hormone, prolactin and oxytocin secretion in ovariectomized, estradiol-treated beef cows following acute weaning. Cutshaw, J.L., Hunter, J.F., Williams, G.L. Theriogenology (1992) [Pubmed]

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