This protein has a length of 421 amino acids, among which, we have to highlight the ATAT1 it is not a modular protein because it only have one It must be highlighted two important regions of ATAT1 (124-137 and 160-269), because is here where junction points with Recently, studies describing the crystal structure of ATAT1 suggest that residues 196 to 236 of human ATAT1 (where acetylated lysines K210 and K221 are located) are disordered and do not contribute significantly to catalytic activity. The difference between isoform 7 and the canonical sequence is that the sequence of amino acids in 195th-218th positions (RPPAPSLRATRHSRAAAVDPTPAA) has been changed by proline (P) and also the sequence 334-421 is missing.Although microtubules usually function as dynamic polymers, for some specific functions they require more stability. Is quite similar to the canonical sequence, the only differences is that the sequence of amino acids in 195th-218th position (RPPAPSLRATRHSRAAAVDPTPAA) is substituted by proline (P).
A complex, regulated folding pathway is required for formation of the αβ-tubulin dimer, complicating attempts at heterologous production of the protein.
A variety of proteins interact with tubulin in the cell, affecting the stability of microtubules and their function. There are some mutations which lead to an increase of activity such as:
The most notable are the alkaloids maytansine, ansamitocin P3, vinblastine and vincristin, which have been shown to be potent inhibitors of tubulin polymerisation in We use cookies to help provide and enhance our service and tailor content and ads. This may occur spontaneously or, on the other hand, due to the action of mutagens.
Isoform 4 is different to the canonical sequence as the sequence of amino acids 323-333 from the canonical chain (RGTPPGLVAQS) has been substituted by a different sequence (SSLPRSEESRY). Reactivity: Hu Species Glossary: Applications: WB, ELISA, PA, AP: Order Details. IHC image of ab7291 staining alpha Tubulin in rat colon formalin fixed paraffin embedded tissue sections, performed on a Leica Bond. ScienceDirect ® is a registered trademark of Elsevier B.V.URL: https://www.sciencedirect.com/science/article/pii/B9780128012383111420URL: https://www.sciencedirect.com/science/article/pii/B9780123786302004795URL: https://www.sciencedirect.com/science/article/pii/B9780128096338080560URL: https://www.sciencedirect.com/science/article/pii/B9780124077577000165URL: https://www.sciencedirect.com/science/article/pii/B9780124076990000029URL: https://www.sciencedirect.com/science/article/pii/S0091679X1095005XURL: https://www.sciencedirect.com/science/article/pii/B9780123943057000033URL: https://www.sciencedirect.com/science/article/pii/B9780323401395000590URL: https://www.sciencedirect.com/science/article/pii/S0165720897800359Encyclopedia of Biological Chemistry (Second Edition)Tubulin and Microtubule Structure: Mechanistic Insights Into Dynamic Instability and Its Biological Relevance☆A Hypothesis on the Origin and Evolution of TubulinCiliary and Flagellar Structure and Function—Their Regulations by Posttranslational Modifications of Axonemal TubulinLafanechère and Job, 2000; Paturle-Lafanechère et al., 1991Congenital Malformations of the Central Nervous SystemApproaches to Design and Synthesis of Antiparasitic DrugsScienceDirect ® is a registered trademark of Elsevier B.V.
In this case, isoform 5 differs to the canonical sequence as the sequence of amino acids 324-421 has been eliminated. Alpha- and beta-tubulin are highly conserved throughout eukaryotes.
These are: This last study allowed to reveal the intracellular distribution of ATAT1 in The immunopositive signal caused by the anti-ATAT1 antibody was observed in epithelial cells of the The α-tubulin N-acetyltransferase is mainly located in In testis, the antibody was observed in spermatocytes and spermatids, but not in sperm. Additionally, the sequence of amino acids 334-421 is missing. Tubulin is the major building block of microtubules. The systematic name of this enzyme class is acetyl-CoA:[alpha-tubulin]-L-lysine N6-acetyltransferase. A complex, regulated folding pathway is required for formation of the αβ-tubulin dimer, complicating attempts at heterologous production of the protein. The binding to α-tubulin at the N-site is nonexchangeable, while the binding to β-tubulin at the E-site is exchangeable. Isoform 6 is probably the isoform which differs the most from the canonical sequence. There are some cases in which the mutation of the gene might cause a reduction in the acetylation of the microtubules. These act as tracks for organelle and macromolecule transport in neurons, and form the structural scaffolds, called axonemes, at the core of beating cilia and flagella (4, 5). The results of these studies will define the currently unknown function of alpha-tubulin in dynamic instability and establish a heretofore missing link between altered in vivo microtubule dynamics and the overall phenotypes of tubulin mutants in yeast.
ATAT1 suffers post translational modifications, which are changes in the protein after it has been translated by ribosomes.For example, abnormal levels of acetylation are closely linked to For some of these diseases a possible solution is an increment of the ATAT1 enzyme.